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
Clathrin
(section)
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!
== Structure == {{Infobox protein | name = [[CLTA (gene)|Clathrin light chain a]] | bodyclass = collapsible collapsed | image = | width = | caption = | Symbol = CLTA | AltSymbols = | IUPHAR_id = | ATC_prefix = | ATC_suffix = | ATC_supplemental = | CAS_number = | CAS_supplemental = | DrugBank = | EntrezGene = 1211 | HGNCid = HGNC:2090. CLTA. | OMIM = | PDB = | RefSeq = | UniProt = P09496 | ECnumber = | Chromosome = 9 | Arm = q | Band = 13 | LocusSupplementaryData = }} {{infobox protein | Name = [[CLTB (gene)|Clathrin light chain b]] | bodyclass = collapsible collapsed | caption = | image = | width = | HGNCid = 2091 | Symbol = CLTB | AltSymbols = | EntrezGene = 1212 | OMIM = 118970 | RefSeq = NM_001834 | UniProt = P09497 | PDB = | ECnumber = | Chromosome = 5 | Arm = q | Band = 35 | LocusSupplementaryData = }} {{infobox protein | Name = [[CLTC|Clathrin heavy chain 1]] | bodyclass = collapsible collapsed | caption = | image = | width = | HGNCid = 2092 | Symbol = CLTC | AltSymbols = CHC, CHC17, CLTCL2 | EntrezGene = 1213 | OMIM = 118955 | RefSeq = NM_004859 | UniProt = Q00610 | PDB = | ECnumber = | Chromosome = 17 | Arm = q | Band = 23.1 | LocusSupplementaryData = -qter }} {{infobox protein | Name = [[CLTCL1|Clathrin heavy chain 2]] | bodyclass = collapsible collapsed | caption = | image = | width = | HGNCid = 2093 | Symbol = CLTCL1 | AltSymbols = CLTCL | EntrezGene = 8218 | OMIM = 601273 | RefSeq = NM_001835 | UniProt = P53675 | PDB = | ECnumber = | Chromosome = 22 | Arm = q | Band = 11.21 | LocusSupplementaryData = }} The clathrin triskelion is composed of three clathrin heavy chains interacting at their [[C-terminus|C-termini]], each ~190 kDa heavy chain has a ~25 kDa light chain tightly bound to it. The three heavy chains provide the structural backbone of the clathrin lattice, and the three light chains are thought to regulate the formation and disassembly of a clathrin lattice. There are two forms of clathrin light chains, designated a and b. The main clathrin heavy chain, located on [[Chromosome 17 (human)|chromosome 17]] in humans, is found in all cells. A second clathrin heavy chain gene, on [[chromosome 22 (human)|chromosome 22]], is expressed in muscle.<ref name="pmid26403691">{{cite journal |vauthors=Robinson MS |title=Forty Years of Clathrin-coated Vesicles |journal=Traffic |volume=16 |issue=12 |pages=1210β38 |date=December 2015 |pmid=26403691 |doi=10.1111/tra.12335 |url=|doi-access=free }}</ref> Clathrin heavy chain is often described as a leg, with subdomains, representing the foot (the [[N-terminal]] domain), followed by the ankle, distal leg, knee, proximal leg, and trimerization domains. The N-terminal domain consists of a seven-bladed Ξ²-propeller structure. The other domains form a super-helix of short alpha helices. This was originally determined from the structure of the proximal leg domain that identified and is composed of a smaller structural module referred to as clathrin heavy chain repeat motifs. The light chains bind primarily to the proximal leg portion of the heavy chain with some interaction near the trimerization domain. The Ξ²-propeller at the 'foot' of clathrin contains multiple binding sites for interaction with other proteins.<ref name="pmid26403691">{{cite journal |vauthors=Robinson MS |title=Forty Years of Clathrin-coated Vesicles |journal=Traffic |volume=16 |issue=12 |pages=1210β38 |date=December 2015 |pmid=26403691 |doi=10.1111/tra.12335 |url=|doi-access=free }}</ref> {{multiple image <!-- Layout parameters --> | align = center | total_width = 440 <!--image 1--> | image1 = Clathrin cage viewed by croelectron microscopy.jpg | caption1 = A clathrin cage with a single triskelion highlighted in blue. CryoEM map EMD_5119 was rendered in UCSF Chimera and one clathrin triskelion was highlighted. <!--image 2--> | image2 = Geometries of common clathrin assemblies.svg | alt2 = | link2 = | thumbtime2 = | caption2 = Each cage has 12 pentagons. Mini-coat (left) has 4 hexagons and tetrahedral symmetry as in a truncated triakis tetrahedron. Hexagonal barrel (middle) has 8 hexagons and D6 symmetry. Soccer ball (right) has 20 hexagons and icosahedral symmetry as in a truncated icosahedron. }} When triskelia assemble together in solution, they can interact with enough flexibility to form 6-sided rings ([[hexagons]]) that yield a flat lattice, or 5-sided rings ([[pentagons]]) that are necessary for curved lattice formation. When many triskelions connect, they can form a basket-like structure. The structure shown, is built of 36 triskelia, one of which is shown in blue. Another common assembly is a [[truncated icosahedron]]. To enclose a vesicle, exactly 12 pentagons must be present in the lattice. In a cell, clathrin triskelion in the cytoplasm binds to an adaptor protein that has bound membrane, linking one of its three feet to the membrane at a time. Clathrin cannot bind to membrane or cargo directly and instead uses adaptor proteins to do this. This triskelion will bind to other membrane-attached triskelia to form a rounded lattice of hexagons and pentagons, reminiscent of the panels on a soccer ball, that pulls the membrane into a bud. By constructing different combinations of 5-sided and 6-sided rings, vesicles of different sizes may assemble. The smallest clathrin cage commonly imaged, called a mini-coat, has 12 pentagons and only two hexagons. Even smaller cages with zero hexagons probably do not form from the native protein, because the feet of the triskelia are too bulky.<ref name="pmid16908193">{{cite journal |vauthors=Fotin A, Kirchhausen T, Grigorieff N, Harrison SC, Walz T, Cheng Y |title=Structure determination of clathrin coats to subnanometer resolution by single particle cryo-electron microscopy |journal=J Struct Biol |volume=156 |issue=3 |pages=453β60 |date=December 2006 |pmid=16908193 |pmc=2910098 |doi=10.1016/j.jsb.2006.07.001 |url=}}</ref>
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)