Open main menu
Home
Random
Recent changes
Special pages
Community portal
Preferences
About Wikipedia
Disclaimers
Incubator escapee wiki
Search
User menu
Talk
Dark mode
Contributions
Create account
Log in
Editing
Golgi apparatus
Warning:
You are not logged in. Your IP address will be publicly visible if you make any edits. If you
log in
or
create an account
, your edits will be attributed to your username, along with other benefits.
Anti-spam check. Do
not
fill this in!
{{Short description|Cell organelle that packages proteins for export}} {{Hatnote group| {{Distinguish|gyrification}} {{For|the song|Junta (album)}} }} {{pp-move-indef|small=yes}} [[File:Golgi apparatus (borderless version)-en.svg|thumb|300px|Diagram of a single "stack" of Golgi]] {{Organelle diagram}} The '''Golgi apparatus''' ({{IPAc-en|ˈ|ɡ|ɒ|l|dʒ|i}}), also known as the '''Golgi complex''', '''Golgi body''', or simply the '''Golgi''', is an [[organelle]] found in most [[eukaryotic]] [[Cell (biology)|cells]].<ref name="Pavelk-2008">{{cite book|title=The Golgi Apparatus: State of the art 110 years after Camillo Golgi's discovery|vauthors=Pavelk M, Mironov AA|publisher=Springer|year=2008|isbn=978-3-211-76310-0|location=Berlin|page=580|doi=10.1007/978-3-211-76310-0_34|chapter=Golgi apparatus inheritance}}</ref> Part of the [[endomembrane system]] in the [[cytoplasm]], it [[protein targeting|packages proteins]] into [[membrane-bound]] [[Vesicle (biology and chemistry)|vesicle]]s inside the cell before the vesicles are sent to their destination. It resides at the intersection of the secretory, lysosomal, and [[Endocytosis|endocytic]] pathways. It is of particular importance in processing [[protein]]s for [[secretion]], containing a set of [[glycosylation]] [[enzyme]]s that attach various sugar monomers to proteins as the proteins move through the apparatus. The Golgi apparatus was identified in 1898 by the Italian biologist and pathologist [[Camillo Golgi]].<ref name="Fabene-1998">{{cite journal|vauthors=Fabene PF, Bentivoglio M|date=October 1998|title=1898-1998: Camillo Golgi and "the Golgi": one hundred years of terminological clones|journal=Brain Research Bulletin|volume=47|issue=3|pages=195–8|doi=10.1016/S0361-9230(98)00079-3|pmid=9865849|s2cid=208785591 }}</ref> The organelle was later named after him in the 1910s.<ref name="Fabene-1998" /> == Discovery == Because of its large size and distinctive structure, the Golgi apparatus was one of the first organelles to be discovered and observed in detail. It was discovered in 1898 by Italian physician Camillo Golgi during an investigation of the [[nervous system]].<ref>{{cite journal | vauthors = Golgi C | year = 1898 | title = Intorno alla struttura delle cellule nervose | url = http://ppp.unipv.it/camillogolgi/pdf/Intornoallastrutturadellecellulenervose.pdf | journal = Bollettino della Società Medico-Chirurgica di Pavia | volume = 13 | issue = 1 | page = 316 | url-status = live | archive-url = https://web.archive.org/web/20180407120042/http://ppp.unipv.it/camillogolgi/pdf/Intornoallastrutturadellecellulenervose.pdf | archive-date = 2018-04-07 }}</ref><ref name="Fabene-1998"/> After first observing it under his [[microscope]], he termed the structure as ''apparato reticolare interno'' ("internal reticular apparatus"). Some doubted the discovery at first, arguing that the appearance of the structure was merely an optical illusion created by Golgi's observation technique. With the development of modern microscopes in the twentieth century, the discovery was confirmed.<ref name="Davidson-2004">{{cite web | url = http://micro.magnet.fsu.edu/cells/golgi/golgiapparatus.html | title = The Golgi Apparatus | author = Davidson MW | date = 2004-12-13 | work = Molecular Expressions | publisher = Florida State University | access-date = 2010-09-20 | url-status = live | archive-url = https://web.archive.org/web/20061107142553/http://micro.magnet.fsu.edu/cells/golgi/golgiapparatus.html | archive-date = 2006-11-07 }}</ref> Early references to the Golgi apparatus referred to it by various names, including the Golgi–Holmgren apparatus, Golgi–Holmgren ducts, and Golgi–Kopsch apparatus.<ref name="Fabene-1998"/> The term Golgi apparatus was used in 1910 and first appeared in scientific literature in 1913, while "Golgi complex" was introduced in 1956.<ref name="Fabene-1998"/> == Subcellular localization == The subcellular localization of the Golgi apparatus varies among eukaryotes. In mammals, a single Golgi apparatus is usually located near the cell nucleus, close to the centrosome. Tubular connections are responsible for linking the stacks together. Localization and tubular connections of the Golgi apparatus are dependent on [[microtubule]]s. In experiments, it is seen that as microtubules are depolymerized, the Golgi apparatuses lose mutual connections and become individual stacks throughout the cytoplasm.<ref name="Alberts-1994">{{cite book| title=Molecular Biology of the Cell| url=https://archive.org/details/molecularbiology00albe| last=Alberts| first=Bruce| publisher=Garland Publishing| isbn=978-0-8153-1619-0| display-authors=etal| year=1994| url-access=registration}}</ref> In [[yeast]], multiple Golgi apparatuses are scattered throughout the cytoplasm (as observed in ''[[Saccharomyces cerevisiae]]''). In [[plant]]s, Golgi stacks are not concentrated at the centrosomal region and do not form Golgi ribbons.<ref name="Nakano-2010">{{cite journal | vauthors = Nakano A, Luini A | title = Passage through the Golgi | journal = Current Opinion in Cell Biology | volume = 22 | issue = 4 | pages = 471–8 | date = August 2010 | pmid = 20605430 | doi = 10.1016/j.ceb.2010.05.003 }}</ref> Organization of the plant Golgi depends on [[actin]] cables and not microtubules.<ref name="Nakano-2010"/> The common feature among Golgi is that they are adjacent to [[endoplasmic reticulum]] (ER) exit sites.<ref name="Suda-2012">{{cite journal | vauthors = Suda Y, Nakano A | title = The yeast Golgi apparatus | journal = Traffic | volume = 13 | issue = 4 | pages = 505–10 | date = April 2012 | pmid = 22132734 | doi = 10.1111/j.1600-0854.2011.01316.x | doi-access = free }}</ref> == Structure == [[File:Blausen 0435 GolgiApparatus.png|thumb|left|3D rendering of Golgi apparatus]] In most eukaryotes, the Golgi apparatus is made up of a series of compartments and is a collection of fused, flattened membrane-enclosed disks known as [[cisternae]] (singular: ''cisterna'', also called "dictyosomes"), originating from vesicular clusters that bud off the endoplasmic reticulum (ER). A mammalian cell typically contains 40 to 100 stacks of cisternae.<ref name="Duran-2008">{{cite journal | vauthors = Duran JM, Kinseth M, Bossard C, Rose DW, Polishchuk R, Wu CC, Yates J, Zimmerman T, Malhotra V | title = The role of GRASP55 in Golgi fragmentation and entry of cells into mitosis | journal = Molecular Biology of the Cell | volume = 19 | issue = 6 | pages = 2579–87 | date = June 2008 | pmid = 18385516 | pmc = 2397314 | doi = 10.1091/mbc.E07-10-0998 }}</ref> Between four and eight cisternae are usually present in a stack; however, in some [[protists]], as many as sixty cisternae have been observed.<ref name="Davidson-2004"/> This collection of cisternae is broken down into ''cis'', medial, and ''trans'' compartments, making up two main networks: the '''cis Golgi network''' (CGN) and the '''trans Golgi network''' (TGN). The CGN is the first cisternal structure, and the TGN is the final, from which proteins are packaged into [[Vesicle (biology and chemistry)|vesicle]]s destined to [[lysosome]]s, secretory vesicles, or the cell surface. The TGN is usually positioned adjacent to the stack, but can also be separate from it. The TGN may act as an early [[endosome]] in yeast and plants.<ref name="Nakano-2010"/><ref name="Day-2018">{{cite journal|doi=10.1016/j.devcel.2017.12.014|pmid=29316441|pmc=5765772|title=Budding Yeast Has a Minimal Endomembrane System|journal=Developmental Cell|volume=44|issue=1|pages=56–72.e4|year=2018|last1=Day|first1=Kasey J.|last2=Casler|first2=Jason C.|last3=Glick|first3=Benjamin S.}}</ref> There are structural and organizational differences in the Golgi apparatus among eukaryotes. In some yeasts, Golgi stacking is not observed. ''[[Pichia pastoris]]'' does have stacked Golgi, while ''Saccharomyces cerevisiae'' does not.<ref name="Nakano-2010"/> In plants, the individual stacks of the Golgi apparatus seem to operate independently.<ref name="Nakano-2010"/> The Golgi apparatus tends to be larger and more numerous in cells that synthesize and secrete large amounts of substances; for example, the [[antibody]]-secreting [[plasma B cell]]s of the immune system have prominent Golgi complexes.{{cn|date=May 2025}} In all eukaryotes, each cisternal stack has a ''cis'' entry face and a ''trans'' exit face. These faces are characterized by unique morphology and [[biochemistry]].<ref name="Day-2013">{{cite journal|author2-link=Lucas Andrew Staehelin | vauthors = Day KJ, Staehelin LA, Glick BS | title = A three-stage model of Golgi structure and function | journal = Histochemistry and Cell Biology | volume = 140 | issue = 3 | pages = 239–49 | date = September 2013 | pmid = 23881164 | pmc = 3779436 | doi = 10.1007/s00418-013-1128-3 }}</ref> Within individual stacks are assortments of enzymes responsible for selectively modifying protein cargo. These modifications influence the fate of the protein. The compartmentalization of the Golgi apparatus is advantageous for separating enzymes, thereby maintaining consecutive and selective processing steps: enzymes catalyzing early modifications are gathered in the ''cis'' face cisternae, and enzymes catalyzing later modifications are found in ''trans'' face cisternae of the Golgi stacks.<ref name="Alberts-1994"/><ref name="Day-2013"/> == Function == [[File:0314 Golgi Apparatus a en.png|thumb|400px|The Golgi apparatus (salmon pink) in context of the secretory pathway]] The Golgi apparatus is a major collection and dispatch station of protein products received from the endoplasmic reticulum. Proteins synthesized in the ER are packaged into vesicles, which then fuse with the Golgi apparatus. These cargo proteins are modified and destined for secretion via [[exocytosis]] or for use in the cell. In this respect, the Golgi can be thought of as similar to a post office: it packages and labels items which it then sends to different parts of the cell or to the [[extracellular space]]. The Golgi apparatus is also involved in [[lipid]] transport and lysosome formation.<ref name="Campbell-1996">{{cite book | first = Neil A | last = Campbell| title = Biology | url = https://archive.org/details/biologycamp00camp | url-access = registration | edition = 4| publisher = Benjamin/Cummings | location = Menlo Park, CA| year = 1996 | pages = [https://archive.org/details/biologycamp00camp/page/122 122], 123| isbn = 978-0-8053-1957-6}}</ref> The structure and function of the Golgi apparatus are intimately linked. Individual stacks have different assortments of enzymes, allowing for progressive processing of cargo proteins as they travel from the cisternae to the trans Golgi face.<ref name="Alberts-1994"/><ref name="Day-2013"/> Enzymatic reactions within the Golgi stacks occur exclusively near its membrane surfaces, where enzymes are anchored. This feature is in contrast to the ER, which has soluble proteins and enzymes in its [[Lumen (anatomy)|lumen]]. Much of the enzymatic processing is [[post-translational modification]] of proteins. For example, phosphorylation of [[oligosaccharide]]s on lysosomal proteins occurs in the early CGN.<ref name="Alberts-1994"/> ''Cis'' [[cisterna]] are associated with the removal of [[mannose]] residues.<ref name="Alberts-1994"/><ref name="Day-2013"/> Removal of mannose residues and addition of [[N-acetylglucosamine]] occur in medial cisternae.<ref name="Alberts-1994"/> Addition of [[galactose]] and [[sialic acid]] occurs in the ''trans'' cisternae.<ref name="Alberts-1994"/> [[Sulfation]] of [[tyrosine]]s and [[carbohydrate]]s occurs within the TGN.<ref name="Alberts-1994"/> Other general post-translational modifications of proteins include the addition of carbohydrates ([[glycosylation]])<ref name="Flynne-2008">{{cite book|author=William G. Flynne|title=Biotechnology and Bioengineering|url=https://books.google.com/books?id=WEBBP5IYqJQC&pg=PA45|access-date=13 November 2010|year=2008|publisher=Nova Publishers|isbn=978-1-60456-067-1|pages=45–}}</ref> and phosphates ([[phosphorylation]]). Protein modifications may form a [[Signal peptide|signal sequence]] that determines the final destination of the protein. For example, the Golgi apparatus adds a [[mannose-6-phosphate]] label to proteins destined for lysosomes. Another important function of the Golgi apparatus is in the formation of [[proteoglycans]]. Enzymes in the Golgi append proteins to [[glycosaminoglycan]]s, thus creating proteoglycans.<ref name="Prydz-2000">{{cite journal | vauthors = Prydz K, Dalen KT | title = Synthesis and sorting of proteoglycans | journal = Journal of Cell Science | volume = 113 Pt 2 | pages = 193–205 | date = January 2000 | pmid = 10633071 | series = 113 | issue = 2 | doi = 10.1242/jcs.113.2.193 | doi-access = free }}</ref> Glycosaminoglycans are long unbranched [[polysaccharide]] molecules present in the [[extracellular matrix]] of animals. == Vesicular transport == [[Image:Nucleus ER golgi.svg|thumb|315px|Diagram of secretory process from endoplasmic reticulum (orange) to Golgi apparatus (magenta). 1. [[Nuclear membrane]]; 2. [[Nuclear pore]]; 3. Rough endoplasmic reticulum (RER); 4. Smooth endoplasmic reticulum (SER); 5. [[Ribosome]] attached to RER; 6. [[Macromolecule]]s; 7. Transport vesicles; 8. Golgi apparatus; 9. ''Cis'' face of Golgi apparatus; 10. ''Trans'' face of Golgi apparatus; 11. Cisternae of the Golgi apparatus.]] The vesicles that leave the [[Endoplasmic reticulum#Rough endoplasmic reticulum|rough endoplasmic reticulum]] are transported to the ''cis'' face of the Golgi apparatus, where they fuse with the Golgi membrane and empty their contents into the [[Lumen (anatomy)|lumen]]. Once inside the lumen, the molecules are modified, then sorted for transport to their next destinations.{{cn|date=May 2025}} Those proteins destined for areas of the cell other than either the endoplasmic reticulum or the Golgi apparatus are moved through the Golgi cisternae towards the ''trans'' face, to a complex network of membranes and associated vesicles known as the ''trans-Golgi network'' (TGN). This area of the Golgi is the point at which proteins are sorted and shipped to their intended destinations by their placement into one of at least three different types of vesicles, depending upon the [[signal peptide|signal sequence]] they carry. {| class="wikitable" ! Types ! Description ! Example |- ! Exocytotic vesicles ''(constitutive)'' | Vesicle contains proteins destined for [[extracellular]] release. After packaging, the vesicles bud off and immediately move towards the [[plasma membrane]], where they fuse and release the contents into the extracellular space in a process known as ''[[Secretory pathway|constitutive secretion]]''. | Antibody release by activated plasma B cells |- ! Secretory vesicles ''(regulated)'' | Vesicles contain proteins destined for extracellular release. After packaging, the vesicles bud off and are stored in the cell until a signal is given for their release. When the appropriate signal is received they move toward the membrane and fuse to release their contents. This process is known as ''[[Secretory pathway|regulated secretion]]''. | [[Neurotransmitter]] release from [[neuron]]s |- ! Lysosomal vesicles | Vesicles contain proteins and ribosomes destined for the lysosome, a degradative organelle containing many acid [[hydrolase]]s, or to lysosome-like storage organelles. These proteins include both digestive enzymes and membrane proteins. The vesicle first fuses with the [[endosome|late endosome]], and the contents are then transferred to the lysosome via unknown mechanisms. | Digestive [[protease]]s destined for the lysosome |} == Current models of vesicular transport and trafficking == {{unsolved|biology|In cell theory, what is the exact transport mechanism by which proteins travel through the Golgi apparatus?}} === Model 1: Anterograde vesicular transport between stable compartments === * In this model, the Golgi is viewed as a set of stable compartments that work together. Each compartment has a unique collection of enzymes that work to modify protein cargo. Proteins are delivered from the ER to the ''cis'' face using [[COPII]]-coated vesicles. Cargo then progress toward the ''trans'' face in [[COPI]]-coated vesicles. This model proposes that COPI vesicles move in two directions: [[Axoplasmic transport#Anterograde transport|anterograde]] vesicles carry [[secretory protein]]s, while [[Axoplasmic transport#Retrograde transport|retrograde]] vesicles recycle Golgi-specific trafficking proteins.<ref name="Glick-2011">{{cite journal | vauthors = Glick BS, Luini A | title = Models for Golgi traffic: a critical assessment | journal = Cold Spring Harbor Perspectives in Biology | volume = 3 | issue = 11 | pages = a005215 | date = November 2011 | pmid = 21875986 | pmc = 3220355 | doi = 10.1101/cshperspect.a005215 }}</ref> ** '''Strengths:''' The model explains observations of compartments, polarized distribution of enzymes, and waves of moving vesicles. It also attempts to explain how Golgi-specific enzymes are recycled.<ref name="Glick-2011"/> ** '''Weaknesses:''' Since the amount of COPI vesicles varies drastically among types of cells, this model cannot easily explain high trafficking activity within the Golgi for both small and large cargoes. Additionally, there is no convincing evidence that COPI vesicles move in both the anterograde and retrograde directions.<ref name="Glick-2011"/> * This model was widely accepted from the early 1980s until the late 1990s.<ref name="Glick-2011"/> ===Model 2: Cisternal progression/maturation=== * In this model, the fusion of COPII vesicles from the ER begins the formation of the first ''cis''-cisterna of the Golgi stack, which progresses later to become mature TGN cisternae. Once matured, the TGN cisternae dissolve to become secretory vesicles. While this progression occurs, COPI vesicles continually recycle Golgi-specific proteins by delivery from older to younger cisternae. Different recycling patterns may account for the differing biochemistry throughout the Golgi stack. Thus, the compartments within the Golgi are seen as discrete kinetic stages of the maturing Golgi apparatus.<ref name="Glick-2011"/> ** '''Strengths:''' The model addresses the existence of Golgi compartments, as well as differing biochemistry within the cisternae, transport of large proteins, transient formation and disintegration of the cisternae, and retrograde mobility of native Golgi proteins, and it can account for the variability seen in the structures of the Golgi.<ref name="Glick-2011"/> ** '''Weaknesses:''' This model cannot easily explain the observation of fused Golgi networks, tubular connections among cisternae, and differing kinetics of secretory cargo exit.<ref name="Glick-2011"/> ===Model 3: Cisternal progression/maturation with heterotypic tubular transport=== * This model is an extension of the cisternal progression/maturation model. It incorporates the existence of tubular connections among the cisternae that form the Golgi ribbon, in which cisternae within a stack are linked. This model posits that the tubules are important for bidirectional traffic in the ER-Golgi system: they allow for fast anterograde traffic of small cargo and/or the retrograde traffic of native Golgi proteins.<ref name="Glick-2011"/><ref name="Wei-2010">{{cite journal |vauthors=Wei JH, Seemann J |title=Unraveling the Golgi ribbon |journal=Traffic |volume=11 |issue=11 |pages=1391–400 |date=November 2010 |pmid=21040294 |pmc=4221251 |doi=10.1111/j.1600-0854.2010.01114.x |url=}}</ref> ** '''Strengths:''' This model encompasses the strengths of the cisternal progression/maturation model that also explains rapid trafficking of cargo, and how native Golgi proteins can recycle independently of COPI vesicles.<ref name="Glick-2011"/> ** '''Weaknesses:''' This model cannot explain the transport kinetics of large protein cargo, such as [[collagen]]. Additionally, tubular connections are not prevalent in plant cells. The roles that these connections have can be attributed to a cell-specific specialization rather than a universal trait. If the membranes are continuous, that suggests the existence of mechanisms that preserve the unique biochemical gradients observed throughout the Golgi apparatus.<ref name="Glick-2011"/> ===Model 4: Rapid partitioning in a mixed Golgi=== * This rapid partitioning model is the most drastic alteration of the traditional vesicular trafficking point of view. Proponents of this model hypothesize that the Golgi works as a single unit, containing domains that function separately in the processing and export of protein cargo. Cargo from the ER move between these two domains, and randomly exit from any level of the Golgi to their final location. This model is supported by the observation that cargo exits the Golgi in a pattern best described by exponential kinetics. The existence of domains is supported by fluorescence microscopy data.<ref name="Glick-2011"/> ** '''Strengths:''' Notably, this model explains the exponential kinetics of cargo exit of both large and small proteins, whereas other models cannot.<ref name="Glick-2011"/> ** '''Weaknesses:''' This model cannot explain the transport kinetics of large protein cargo, such as collagen. This model falls short on explaining the observation of discrete compartments and polarized biochemistry of the Golgi cisternae. It also does not explain formation and disintegration of the Golgi network, nor the role of COPI vesicles.<ref name="Glick-2011"/> ===Model 5: Stable compartments as cisternal model progenitors=== * This is the most recent model. In this model, the Golgi is seen as a collection of stable compartments defined by [[Rab (G-protein)]] [[GTPase]]s.<ref name="Glick-2011"/> ** '''Strengths:''' This model is consistent with numerous observations and encompasses some of the strengths of the cisternal progression/maturation model. Additionally, what is known of the [[Rab GTPase]] roles in mammalian endosomes can help predict putative roles within the Golgi. This model is unique in that it can explain the observation of "megavesicle" transport intermediates.<ref name="Glick-2011"/> ** '''Weaknesses:''' This model does not explain morphological variations in the Golgi apparatus, nor define a role for COPI vesicles. This model does not apply well for plants, algae, and fungi in which individual Golgi stacks are observed (transfer of domains between stacks is not likely). Additionally, megavesicles are not established to be intra-Golgi transporters.<ref name="Glick-2011"/> Though there are multiple models that attempt to explain vesicular traffic throughout the Golgi, no individual model can independently explain all observations of the Golgi apparatus. Currently, the cisternal progression/maturation model is the most accepted among scientists, accommodating many observations across eukaryotes. The other models are still important in framing questions and guiding future experimentation. Among the fundamental unanswered questions are the directionality of COPI vesicles and role of Rab GTPases in modulating protein cargo traffic.<ref name="Glick-2011"/> == Brefeldin A == [[Brefeldin A]] (BFA) is a fungal [[metabolite]] used experimentally to disrupt the secretion pathway as a method of testing Golgi function.<ref name="Marie-2008">{{cite journal | vauthors = Marie M, Sannerud R, Avsnes Dale H, Saraste J | title = Take the 'A' train: on fast tracks to the cell surface | journal = Cellular and Molecular Life Sciences | volume = 65 | issue = 18 | pages = 2859–74 | date = September 2008 | pmid = 18726174 | doi = 10.1007/s00018-008-8355-0 | pmc = 7079782 }}</ref> BFA blocks the activation of some [[ADP-ribosylation]] factors ([[ADP ribosylation factor|ARF]]s).<ref name="D'Souza-Schorey-2006">{{cite journal | vauthors = D'Souza-Schorey C, Chavrier P | title = ARF proteins: roles in membrane traffic and beyond | journal = Nature Reviews. Molecular Cell Biology | volume = 7 | issue = 5 | pages = 347–58 | date = May 2006 | pmid = 16633337 | doi = 10.1038/nrm1910 | s2cid = 19092867 }}</ref> ARFs are small [[GTPase]]s which regulate vesicular trafficking through the binding of COPs to [[endosome]]s and the Golgi.<ref name="D'Souza-Schorey-2006"/> BFA inhibits the function of several [[guanine nucleotide exchange factor]]s (GEFs) that mediate GTP-binding of ARFs.<ref name="D'Souza-Schorey-2006"/> Treatment of cells with BFA thus disrupts the secretion pathway, promoting disassembly of the Golgi apparatus and distributing Golgi proteins to the endosomes and ER.<ref name="Marie-2008"/><ref name="D'Souza-Schorey-2006"/> == Gallery == <gallery mode="packed"> File:YeastGolgiMovieeLifec.ogg|Yeast Golgi dynamics. Green labels early Golgi, red labels late Golgi.<ref name="Papanikou-2015">{{cite journal | vauthors = Papanikou E, Day KJ, Austin J, Glick BS | title = COPI selectively drives maturation of the early Golgi | journal = eLife | volume = 4 | year = 2015 | pmid = 26709839 | pmc = 4758959 | doi = 10.7554/eLife.13232 | doi-access = free }}</ref> File:GolgiRibbonc.jpg|Two Golgi stacks connected as a ribbon in a mouse cell. Taken from [https://commons.wikimedia.org/wiki/File:Urothelial-Plaque-Formation-in-Post-Golgi-Compartments-pone.0023636.s002.ogv the movie]. File:GolgiScyl1c.jpg|Three-dimensional projection of a mammalian Golgi stack imaged by [[confocal microscopy]] and volume surface rendered using [[Bitplane#Imaris|Imaris]] software. Taken from [[commons:File:Scyl1-Regulates-Golgi-Morphology-pone.0009537.s002.ogv|the movie]]. </gallery> == References == {{Reflist|35em}} == External links == {{Scholia}} * {{Commons category-inline|Golgi apparatus}} {{organelles}} {{Authority control}} {{DEFAULTSORT:Golgi Apparatus}} [[Category:Organelles]] [[Category:Anatomy named for one who described it]]
Edit summary
(Briefly describe your changes)
By publishing changes, you agree to the
Terms of Use
, and you irrevocably agree to release your contribution under the
CC BY-SA 4.0 License
and the
GFDL
. You agree that a hyperlink or URL is sufficient attribution under the Creative Commons license.
Cancel
Editing help
(opens in new window)
Pages transcluded onto the current version of this page
(
help
)
:
Template:Authority control
(
edit
)
Template:Cite book
(
edit
)
Template:Cite journal
(
edit
)
Template:Cite web
(
edit
)
Template:Cn
(
edit
)
Template:Commons category-inline
(
edit
)
Template:Hatnote group
(
edit
)
Template:IPAc-en
(
edit
)
Template:Organelle diagram
(
edit
)
Template:Organelles
(
edit
)
Template:Pp-move-indef
(
edit
)
Template:Reflist
(
edit
)
Template:Scholia
(
edit
)
Template:Short description
(
edit
)
Template:Unsolved
(
edit
)