p24 proteins, intracellular trafficking, and behavior:: Drosophila melanogaster provides insights and opportunities

被引:63
作者
Carney, GE
Bowen, NJ
机构
[1] Georgia Inst Technol, Sch Biol, Atlanta, GA 30332 USA
[2] Univ Georgia, Ovarian Canc Inst, Athens, GA 30602 USA
[3] Univ Georgia, Dept Genet, Athens, GA 30602 USA
关键词
EMP24/GP25; vesicle trafficking; oviposition behavior; phylogeny;
D O I
10.1016/j.biolcel.2004.01.004
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The p24 transmembrane proteins, also known as EMP24/GP25 (endomembrane protein precursor of 24kD (Schimmoller et al., 1995)) proteins, are components of coat protein (COP)-coated vesicles and are present in species as diverse as fungi, plants, flies, worms, and mammals, indicating that they have important conserved functions. Genetic, molecular, and biochemical characterization of these proteins and the loci that encode them has provided insights into their potential cellular roles, including postulated functions in vesicle cargo protein selection and sorting, COPI and COPII vesicle formation and budding, and quality control of proteins that mature through the secretory pathway. Recently, the first mutations in a Drosophila melanogaster p24 gene have been isolated and characterized. These alleles produce an interesting behavioral phenotype in females, affecting their ability to oviposit. This identification and mutant characterization of a p24 locus in Drosophila will pave the way for a better understanding of cell-type-specific functions and interactions among p24 proteins. (C) 2004 Elsevier SAS. All rights reserved.
引用
收藏
页码:271 / 278
页数:8
相关论文
共 34 条
[1]  
Anantharaman V., 2002, GENOME BIOL, V3
[2]   COPII and selective export from the endoplasmic reticulum [J].
Barlowe, C .
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH, 1998, 1404 (1-2) :67-76
[3]  
BARPELED M, 1995, PLANT CELL, V7, P667, DOI 10.1105/tpc.7.6.667
[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]   Coupling of coat assembly and vesicle budding to packaging of putative cargo receptors [J].
Bremser, M ;
Nickel, W ;
Schweikert, M ;
Ravazzola, M ;
Amherdt, M ;
Hughes, CA ;
Söllner, TH ;
Rothman, JE ;
Wieland, FT .
CELL, 1999, 96 (04) :495-506
[6]  
Carney GE, 2003, GENETICS, V164, P173
[7]   Identification of a lumenal sequence specifying the assembly of Emp24p into p24 complexes in the yeast secretory pathway [J].
Ciufo, LF ;
Boyd, A .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (12) :8382-8388
[8]   Characterization of Cop I coat proteins in plant cells [J].
Contreras, I ;
Ortiz-Zapater, E ;
Castilho, LM ;
Aniento, F .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2000, 273 (01) :176-182
[9]   Identification and localization of a β-COP-like protein involved in the morphodynamics of the plant Golgi apparatus [J].
Couchy, I ;
Bolte, S ;
Crosnier, MT ;
Brown, S ;
Satiat-Jeunemaitre, A .
JOURNAL OF EXPERIMENTAL BOTANY, 2003, 54 (390) :2053-2063
[10]   FISSION YEAST AND A PLANT HAVE FUNCTIONAL HOMOLOGS OF THE SAR1-PROTEIN AND SEC12-PROTEIN INVOLVED IN ER TO GOLGI TRAFFIC IN BUDDING YEAST [J].
DENFERT, C ;
GENSSE, M ;
GAILLARDIN, C .
EMBO JOURNAL, 1992, 11 (11) :4205-4211