Submit Data |  Help |  Video Tutorials |  News |  Publications |  FTP Download |  REST API |  Citing RGD |  Contact   

Clathrin light chains LCA and LCB are similar, polymorphic, and share repeated heptad motifs.

Authors: Kirchhausen, T  Scarmato, P  Harrison, SC  Monroe, JJ  Chow, EP  Mattaliano, RJ  Ramachandran, KL  Smart, JE  Ahn, AH  Brosius, J 
Citation: Kirchhausen T, etal., Science 1987 Apr 17;236(4799):320-4.
Pubmed: (View Article at PubMed) PMID:3563513

The clathrin light chains fall into two major classes, LCA and LCB. In an intact clathrin triskelion, one light chain, of either class, is bound to the proximal segment of a heavy chain leg. Analysis of rat brain and liver complementary DNA clones for LCA and LCB shows that the two light chain classes are closely related. There appear to be several members of each class having deletions of varying length aligned at the same position. A set of ten heptad elements, characteristic of alpha-helical coiled coils, is a striking feature of the central part of each derived amino acid sequence. These observations suggest a model in which the alpha-helical segment mediates binding to clathrin heavy chains and the amino- and carboxyl-terminal segments mediate interactions with other proteins. They also suggest an explanation for the observed tissue-dependent size variation for members of each class.


Gene Ontology Annotations
Objects Annotated

Additional Information

CRRD Object Information
CRRD ID: 70686
Created: 2002-06-18
Species: All species
Last Modified: 2002-06-18
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.