scholarly journals Expression of Golgi Membrane Protein p138 is Cell Cycle-independent and Dissociated from Centrosome Duplication

2002 ◽  
Vol 27 (2) ◽  
pp. 117-117 ◽  
Author(s):  
Kohei Doi ◽  
Shohei Noma ◽  
Fumiaki Yamao ◽  
Hideki Goko ◽  
Tatsuo Yagura
Keyword(s):  
Cell Cycle ◽  
Membrane Protein ◽  
Centrosome Duplication ◽  
Golgi Membrane

scholarly journals Phosphorylation of Centrin during the Cell Cycle and Its Role in Centriole Separation Preceding Centrosome Duplication

2001 ◽  
Vol 276 (23) ◽  
pp. 20774-20780 ◽  
Author(s):  
Ward Lutz ◽  
Wilma L. Lingle ◽  
Daniel McCormick ◽  
Tammy M. Greenwood ◽  
Jeffrey L. Salisbury
Keyword(s):  
Cell Cycle ◽  
Centrosome Duplication

scholarly journals A Novel Golgi Membrane Protein Is a Partner of the ARF Exchange Factors Gea1p and Gea2p

2003 ◽  
Vol 14 (6) ◽  
pp. 2357-2371 ◽  
Author(s):  
Sophie Chantalat ◽  
Rëgis Courbeyrette ◽  
Francesca Senic-Matuglia ◽  
Catherine L. Jackson ◽  
Bruno Goud ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Protein Trafficking ◽  
Transmembrane Domain ◽  
Integral Membrane Protein ◽  
Membrane Dynamics ◽  
General Interest ◽  
Single Mutation ◽  
Golgi Membrane ◽  
Nucleotide Exchange

The Sec7 domain guanine nucleotide exchange factors (GEFs) for the GTPase ARF are highly conserved regulators of membrane dynamics and protein trafficking. The interactions of large ARF GEFs with cellular membranes for localization and/or activation are likely to participate in regulated recruitment of ARF and effectors. However, these interactions remain largely unknown. Here we characterize Gmh1p, the first Golgi transmembrane-domain partner of any of the high-molecular-weight ARF-GEFs. Gmh1p is an evolutionarily conserved protein. We demonstrate molecular interaction between the yeast Gmh1p and the large ARF-GEFs Gea1p and Gea2p. This interaction involves a domain of Gea1p and Gea2p that is conserved in the eukaryotic orthologues of the Gea proteins. A single mutation in a conserved amino acid residue of this domain is sufficient to abrogate the interaction, whereas the overexpression of Gmh1p can compensate in vivo defects caused by mutations in this domain. We show that Gmh1p is an integral membrane protein that localizes to the early Golgi in yeast and in human HeLa cells and cycles through the ER. Hence, we propose that Gmh1p acts as a positive Golgi-membrane partner for Gea function. These results are of general interest given the evolutionary conservation of both ARF-GEFs and the Gmh proteins.

The yeast VPS5/GRD2 gene encodes a sorting nexin-1-like protein required for localizing membrane proteins to the late Golgi

1997 ◽  
Vol 110 (9) ◽  
pp. 1063-1072 ◽  
Author(s):  
S.F. Nothwehr ◽  
A.E. Hindes
Keyword(s):  
Membrane Proteins ◽  
Membrane Protein ◽  
Protein Localization ◽  
Endocytic Pathway ◽  
Yeast Cells ◽  
Carboxypeptidase Y ◽  
Golgi Membrane ◽  
Sorting Nexin ◽  
Vacuolar Protein ◽  
Sorting Nexin 1

Genetic analysis of late Golgi membrane protein localization in Saccharomyces cerevisiae has uncovered a large number of genes (called GRD) that are required for retention of A-ALP, a model late Golgi membrane protein. Here we describe one of the GRD genes, VPSS/GRD2, that encodes a hydrophilic protein similar to human sorting nexin-1, a protein involved in trafficking of the epidermal growth factor receptor. In yeast cells containing a vps5 null mutation the late Golgi membrane proteins A-ALP and Kex2p were rapidly mislocalized to the vacuolar membrane. A-ALP was delivered to the vacuole in vps5 mutants in a manner independent of a block in the early endocytic pathway. vps5 null mutants also exhibited defects in both vacuolar morphology and in sorting of a soluble vacuolar protein, carboxypeptidase Y. The latter defect is apparently due to an inability to localize the carboxypeptidase Y sorting receptor, Vps10p, to the Golgi since it is rapidly degraded in the vacuole in vps5 mutants. Fractionation studies indicate that Vps5p is distributed between a free cytosolic pool and a particulate fraction containing Golgi, transport vesicles, and possibly endosomes, but lacking vacuolar membranes. Immunofluorescence microscopy experiments show that the membrane-associated pool of Vps5p localizes to an endosome-like organelle that accumulates in the class E vps27 mutant. These results support a model in which Vps5p is required for retrieval of membrane proteins from a prevacuolar/late endosomal compartment back to the late Golgi apparatus.

Defining the Retention Signal in a Model Golgi Membrane Protein

1993 ◽  
pp. 127-133
Author(s):  
C. E. Machamer ◽  
M. G. Grim ◽  
A. Esquela ◽  
K. Ryan ◽  
A. M. Swift
Keyword(s):  
Membrane Protein ◽  
Golgi Membrane ◽  
Retention Signal

scholarly journals A monoclonal antibody against a 135-K Golgi membrane protein.

1982 ◽  
Vol 1 (12) ◽  
pp. 1621-1628 ◽  
Author(s):  
B. Burke ◽  
G. Griffiths ◽  
H. Reggio ◽  
D. Louvard ◽  
G. Warren
Keyword(s):  
Monoclonal Antibody ◽  
Membrane Protein ◽  
Golgi Membrane
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