Sorting determinants in the transmembrane domain of p24 proteins

被引:46
作者
Fiedler, K
Rothman, JE
机构
[1] Cell. Biochem. and Biophys. Program, Mem. Sloan-Kettering Cancer Center, New York
[2] Cell. Biochem. and Biophys. Program, Mem. Sloan-Kettering Cancer Center, New York, NY 10021
关键词
D O I
10.1074/jbc.272.40.24739
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
Members of the p24 family of putative cargo receptors are proposed to contain retrograde and anterograde trafficking signals in their cytoplasmic domain to facilitate coat protein binding and cycling in the secretory pathway. We have analyzed the role of the transmembrane domain (TMD) of a p24 protein isolated from COPI-coated intra-Golgi transport vesicles. CD8-p24 chimeras were transiently expressed in COS7 cells and analyzed by immunofluorescence and pulse-chase experiments. The localization and transit of the wild-type chimera from the endoplasmic reticulum (ER) through the Golgi complex involved a glutamic acid residue and a conserved glutamine in the TMD. The TMD glutamic acid mediated the localization of the chimeras to the ER in the absence of the conserved glutamine. Efficient ER exit required the TMD glutamine and was further facilitated by a pair of phenylalanine residues in the cytoplasmic bail. TMD residues of p24 proteins may mediate the interaction with integral membrane proteins of the vesicle budding machinery to ensure p24 packaging into transport vesicles.
引用
收藏
页码:24739 / 24742
页数:4
相关论文
共 61 条
[1]   STRUCTURAL REQUIREMENTS OF A MEMBRANE-SPANNING DOMAIN FOR PROTEIN ANCHORING AND CELL-SURFACE TRANSPORT [J].
ADAMS, GA ;
ROSE, JK .
CELL, 1985, 41 (03) :1007-1015
[2]   Principles of selective transport: Coat complexes hold the key [J].
Aridor, M ;
Balch, WE .
TRENDS IN CELL BIOLOGY, 1996, 6 (08) :315-320
[3]   LOCALIZATION OF SED5, A PUTATIVE VESICLE TARGETING MOLECULE, TO THE CIS-GOLGI NETWORK INVOLVES BOTH ITS TRANSMEMBRANE AND CYTOPLASMIC DOMAINS [J].
BANFIELD, DK ;
LEWIS, MJ ;
RABOUILLE, C ;
WARREN, G ;
PELHAM, HRB .
JOURNAL OF CELL BIOLOGY, 1994, 127 (02) :357-371
[4]   Erv25p, a component of COPII-coated vesicles, forms a complex with Emp24p that is required for efficient endoplasmic reticulum to Golgi transport [J].
Belden, WJ ;
Barlowe, C .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (43) :26939-26946
[5]   Tmp21 and p24A, two type I proteins enriched in pancreatic microsomal membranes, are members of a protein family involved in vesicular trafficking [J].
Blum, R ;
Feick, P ;
Puype, M ;
Vandekerckhove, J ;
Klengel, R ;
Nastainczyk, W ;
Schulz, I .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (29) :17183-17189
[6]   KEX2-DEPENDENT INVERTASE SECRETION AS A TOOL TO STUDY THE TARGETING OF TRANSMEMBRANE PROTEINS WHICH ARE INVOLVED IN ER-]GOLGI TRANSPORT IN YEAST [J].
BOEHM, J ;
ULRICH, HD ;
OSSIG, R ;
SCHMITT, HD .
EMBO JOURNAL, 1994, 13 (16) :3696-3710
[7]  
Boehm J, 1997, J CELL SCI, V110, P991
[8]   ROLE OF POTENTIALLY CHARGED TRANSMEMBRANE RESIDUES IN TARGETING PROTEINS FOR RETENTION AND DEGRADATION WITHIN THE ENDOPLASMIC-RETICULUM [J].
BONIFACINO, JS ;
COSSON, P ;
SHAH, N ;
KLAUSNER, RD .
EMBO JOURNAL, 1991, 10 (10) :2783-2793
[9]   COLOCALIZED TRANSMEMBRANE DETERMINANTS FOR ER DEGRADATION AND SUBUNIT ASSEMBLY EXPLAIN THE INTRACELLULAR FATE OF TCR CHAINS [J].
BONIFACINO, JS ;
COSSON, P ;
KLAUSNER, RD .
CELL, 1990, 63 (03) :503-513
[10]   Transmembrane domain sequence requirements for activation of the p185(c-neu) receptor tyrosine kinase [J].
Chen, LI ;
Webster, MK ;
Meyer, AN ;
Donoghue, DJ .
JOURNAL OF CELL BIOLOGY, 1997, 137 (03) :619-631