Ontology highlight
ABSTRACT:
SUBMITTER: Sato K
PROVIDER: S-EPMC2633560 | biostudies-literature | 2009 Jan
REPOSITORIES: biostudies-literature
Sato Ken K Ernstrom Glen G GG Watanabe Shigeki S Weimer Robby M RM Chen Chih-Hsiung CH Sato Miyuki M Siddiqui Ayesha A Jorgensen Erik M EM Grant Barth D BD
Proceedings of the National Academy of Sciences of the United States of America 20090116 4
Clathrin is a coat protein involved in vesicle budding from several membrane-bound compartments within the cell. Here we present an analysis of a temperature-sensitive (ts) mutant of clathrin heavy chain (CHC) in a multicellular animal. As expected Caenorhabditis elegans chc-1(b1025ts) mutant animals are defective in receptor-mediated endocytosis and arrest development soon after being shifted to the restrictive temperature. Steady-state clathrin levels in these mutants are reduced by more than ...[more]