A novel clathrin homolog that co-distributes with cytoskeletal components functions in the trans-Golgi network

被引:48
作者
Liu, SH
Towler, MC
Chen, E
Chen, CY
Song, WX
Apodaca, G
Brodsky, FM [1 ]
机构
[1] Univ Calif San Francisco, GW Hooper Fdn, Dept Microbiol & Immunol, San Francisco, CA 94143 USA
[2] Univ Calif San Francisco, Dept Biopharmaceut Sci, San Francisco, CA 94143 USA
[3] Univ Calif San Francisco, Dept Pharmaceut Chem, San Francisco, CA 94143 USA
[4] Univ Maryland, Dept Mol Genet & Cell Biol, College Pk, MD 20742 USA
[5] Univ Pittsburgh, Dept Med, Div Renal Electrolyte, Pittsburgh, PA 15261 USA
[6] Univ Pittsburgh, Dept Cell Biol & Physiol, Pittsburgh, PA 15261 USA
关键词
clathrin; cytoskeleton; homolog; muscle; trans-Golgi network;
D O I
10.1093/emboj/20.1.272
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A clathrin homolog encoded on human chromosome 22 (CHC22) displays distinct biochemistry, distribution and function compared with conventional clathrin heavy chain (CHC17), encoded on chromosome 17, CHC22 protein is upregulated during myoblast differentiation into myotubes and is expressed at high levels in muscle and at low levels in non-muscle cells, relative to CHC17, The trimeric CHC22 protein does not interact with clathrin heavy chain subunits nor bind significantly to clathrin light chains. CHC22 associates with the AP1 and AP3 adaptor complexes but not with AP2, In non-muscle tells, CHC22 localizes to perinuclear vesicular structures, the majority of which are not clathrin coated, Treatments that disrupt the actin-myosin cytoskeleton or affect sorting in the trans-Golgi network (TGN) cause CHC22 redistribution. Overexpression of a subdomain of CHC22 induces altered distribution of TGN markers. Together these results implicate CHC22 in TGN membrane traffic involving the cytoskeleton.
引用
收藏
页码:272 / 284
页数:13
相关论文
共 46 条
[1]   PREDOMINANCE OF CLATHRIN LIGHT CHAIN LCB CORRELATES WITH THE PRESENCE OF A REGULATED SECRETORY PATHWAY [J].
ACTON, SL ;
BRODSKY, FM .
JOURNAL OF CELL BIOLOGY, 1990, 111 (04) :1419-1426
[2]   Membrane motors [J].
Allan, VJ ;
Schroer, TA .
CURRENT OPINION IN CELL BIOLOGY, 1999, 11 (04) :476-482
[3]   SITE-SPECIFIC DISRUPTION OF CLATHRIN ASSEMBLY PRODUCES NOVEL STRUCTURES [J].
BLANK, GS ;
BRODSKY, FM .
EMBO JOURNAL, 1986, 5 (09) :2087-2095
[4]   Comparative mapping of the DiGeorge syndrome region in mouse shows inconsistent gene order and differential degree of gene conservation [J].
Botta, A ;
Lindsay, EA ;
Jurecic, V ;
Baldini, A .
MAMMALIAN GENOME, 1997, 8 (12) :890-895
[5]   The localization of myosin VI at the Golgi complex and leading edge of fibroblasts and its phosphorylation and recruitment into membrane ruffles of A431 cells after growth factor stimulation [J].
Buss, F ;
Kendrick-Jones, J ;
Lionne, C ;
Knight, AE ;
Côté, GP ;
Luzio, JP .
JOURNAL OF CELL BIOLOGY, 1998, 143 (06) :1535-1545
[6]  
CASPERS P, 1994, CELL MOL BIOL, V40, P635
[7]   100-KDA POLYPEPTIDES IN PERIPHERAL CLATHRIN-COATED VESICLES ARE REQUIRED FOR RECEPTOR-MEDIATED ENDOCYTOSIS [J].
CHIN, DJ ;
STRAUBINGER, RM ;
ACTON, S ;
NATHKE, I ;
BRODSKY, FM .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1989, 86 (23) :9289-9293
[8]   The AP-3 adaptor complex is essential for cargo-selective transport to the yeast vacuole [J].
Cowles, CR ;
Odorizzi, G ;
Payne, GS ;
Emr, SD .
CELL, 1997, 91 (01) :109-118
[9]   AP-4, a novel protein complex related to clathrin adaptors [J].
Dell'Angelica, EC ;
Mullins, C ;
Bonifacino, JS .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (11) :7278-7285
[10]   Association of the AP-3 adaptor complex with clathrin [J].
Dell'Angelica, EC ;
Klumperman, J ;
Stoorvogel, W ;
Bonifacino, JS .
SCIENCE, 1998, 280 (5362) :431-434