Huntingtin-interacting protein 1 (Hip1) and Hip1-related protein (Hip1R) bind the conserved sequence of clathrin light chains and thereby influence clathrin assembly in vitro and actin distribution in vivo

被引:90
作者
Chen, CY
Brodsky, FM [1 ]
机构
[1] Univ Calif San Francisco, George Williams Hooper Fdn, Dept Biopharmaceut Sci, San Francisco, CA 94143 USA
[2] Univ Calif San Francisco, Dept Microbiol & Immunol, San Francisco, CA 94143 USA
[3] Univ Calif San Francisco, Dept Pharmaceut Chem, San Francisco, CA 94143 USA
关键词
D O I
10.1074/jbc.M408454200
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
Clathrin heavy and light chains form triskelia, which assemble into polyhedral coats of membrane vesicles that mediate transport for endocytosis and organelle biogenesis. Light chain subunits regulate clathrin assembly in vitro by suppressing spontaneous self-assembly of the heavy chains. The residues that play this regulatory role are at the N terminus of a conserved 22-amino acid sequence that is shared by all vertebrate light chains. Here we show that these regulatory residues and others in the conserved sequence mediate light chain interaction with Hip1 and Hip1R. These related proteins were previously found to be enriched in clathrin-coated vesicles and to promote clathrin assembly in vitro. We demonstrate Hip1R binding preference for light chains associated with clathrin heavy chain and show that Hip1R stimulation of clathrin assembly in vitro is blocked by mutations in the conserved sequence of light chains that abolish interaction with Hip1 and Hip1R. In vivo overexpression of a fragment of clathrin light chain comprising the Hip1R-binding region affected cellular actin distribution. Together these results suggest that the roles of Hip1 and Hip1R in affecting clathrin assembly and actin distribution are mediated by their interaction with the conserved sequence of clathrin light chains.
引用
收藏
页码:6109 / 6117
页数:9
相关论文
共 42 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]   ALTERATION OF CLATHRIN LIGHT-CHAIN EXPRESSION BY TRANSFECTION AND GENE DISRUPTION [J].
ACTON, SL ;
WONG, DH ;
PARHAM, P ;
BRODSKY, FM ;
JACKSON, AP .
MOLECULAR BIOLOGY OF THE CELL, 1993, 4 (06) :647-660
[3]   Clathrin Hub expression dissociates the actin-binding protein Hip1R from coated pits and disrupts their alignment with the actin cytoskeleton [J].
Bennett, EM ;
Chen, CY ;
Engqvist-Goldstein, ÅEY ;
Drubin, DG ;
Brodsky, FM .
TRAFFIC, 2001, 2 (11) :851-858
[4]   Signals for sorting of transmembrane proteins to endosomes and lysosomes [J].
Bonifacino, JS ;
Traub, LM .
ANNUAL REVIEW OF BIOCHEMISTRY, 2003, 72 :395-447
[5]   CLATHRIN LIGHT-CHAINS - ARRAYS OF PROTEIN MOTIFS THAT REGULATE COATED-VESICLE DYNAMICS [J].
BRODSKY, FM ;
HILL, BL ;
ACTON, SL ;
NATHKE, I ;
WONG, DH ;
PONNAMBALAM, S ;
PARHAM, P .
TRENDS IN BIOCHEMICAL SCIENCES, 1991, 16 (06) :208-213
[6]   Biological basket weaving: Formation and function of clathrin-coated vesicles [J].
Brodsky, FM ;
Chen, CY ;
Knuehl, C ;
Towler, MC ;
Wakeham, DE .
ANNUAL REVIEW OF CELL AND DEVELOPMENTAL BIOLOGY, 2001, 17 :517-568
[7]   Cortactin is a component of clathrin-coated pits and participates in receptor-mediated endocytosis [J].
Cao, H ;
Orth, JD ;
Chen, J ;
Weller, SG ;
Heuser, JE ;
McNiven, MA .
MOLECULAR AND CELLULAR BIOLOGY, 2003, 23 (06) :2162-2170
[8]   Actin dynamics coupled to clathrin-coated vesicle formation at the trans-Golgi network [J].
Carreno, S ;
Engqvist-Goldstein, ÅE ;
Zhang, CX ;
McDonald, KL ;
Drubin, DG .
JOURNAL OF CELL BIOLOGY, 2004, 165 (06) :781-788
[9]   Clathrin light and heavy chain interface:: α-helix binding superhelix loops via critical tryptophans [J].
Chen, CY ;
Reese, ML ;
Hwang, PK ;
Ota, N ;
Agard, D ;
Brodsky, FM .
EMBO JOURNAL, 2002, 21 (22) :6072-6082
[10]   Regulated portals of entry into the cell [J].
Conner, SD ;
Schmid, SL .
NATURE, 2003, 422 (6927) :37-44