Molecular cloning of YPT1/SEC4-related cDNAs from an epithelial cell line

1990 ◽  
Vol 10 (12) ◽  
pp. 6578-6585
Author(s):  
P Chavrier ◽  
M Vingron ◽  
C Sander ◽  
K Simons ◽  
M Zerial
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Binding Proteins ◽  
Membrane Traffic ◽  
Epithelial Cell Line ◽  
Madin Darby Canine Kidney ◽  
Gtp Binding Proteins ◽  
Gtp Binding ◽  
High Level ◽  
Darby Canine Kidney ◽  
Canine Kidney

Molecular analysis of Saccharomyces cerevisiae secretion mutants has led to the identification of two Ras-like GTP-binding proteins, Ypt1p and Sec4p, which are essential for transport along the exocytic route. To study the regulation of membrane traffic in epithelial cells, a set of 11 clones encoding proteins similar to the YPT1/SEC4 products were isolated from an MDCK (Madin-Darby canine kidney) cell cDNA library. Four of these proteins, Rab8, -9, -10, and -11, are novel members of this subfamily of Ras-like proteins, and two of them are closely related to Ypt1p and Sec4p. The ratio of the number of clones isolated over the total number screened reveals a high level of complexity for this subfamily of GTP-binding proteins. This diversity supports their proposed function in controlling different steps in membrane traffic.

scholarly journals Molecular cloning of YPT1/SEC4-related cDNAs from an epithelial cell line.

1990 ◽  
Vol 10 (12) ◽  
pp. 6578-6585 ◽  
Author(s):  
P Chavrier ◽  
M Vingron ◽  
C Sander ◽  
K Simons ◽  
M Zerial
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Binding Proteins ◽  
Membrane Traffic ◽  
Epithelial Cell Line ◽  
Madin Darby Canine Kidney ◽  
Gtp Binding Proteins ◽  
Gtp Binding ◽  
High Level ◽  
Darby Canine Kidney ◽  
Canine Kidney

Molecular analysis of Saccharomyces cerevisiae secretion mutants has led to the identification of two Ras-like GTP-binding proteins, Ypt1p and Sec4p, which are essential for transport along the exocytic route. To study the regulation of membrane traffic in epithelial cells, a set of 11 clones encoding proteins similar to the YPT1/SEC4 products were isolated from an MDCK (Madin-Darby canine kidney) cell cDNA library. Four of these proteins, Rab8, -9, -10, and -11, are novel members of this subfamily of Ras-like proteins, and two of them are closely related to Ypt1p and Sec4p. The ratio of the number of clones isolated over the total number screened reveals a high level of complexity for this subfamily of GTP-binding proteins. This diversity supports their proposed function in controlling different steps in membrane traffic.

scholarly journals Association of Rab25 and Rab11a with the Apical Recycling System of Polarized Madin–Darby Canine Kidney Cells

1999 ◽  
Vol 10 (1) ◽  
pp. 47-61 ◽  
Author(s):  
James E. Casanova ◽  
Xiaoye Wang ◽  
Ravindra Kumar ◽  
Sheela G. Bhartur ◽  
Jennifer Navarre ◽  
...  
Keyword(s):  
Mdck Cells ◽  
Basolateral Membrane ◽  
Dominant Negative ◽  
Epithelial Cell Line ◽  
Madin Darby Canine Kidney ◽  
Recycling Endosome ◽  
Recycling System ◽  
Endosomal Compartment ◽  
Darby Canine Kidney ◽  
Canine Kidney

Recent evidence suggests that apical and basolateral endocytic pathways in epithelia converge in an apically located, pericentriolar endosomal compartment termed the apical recycling endosome. In this compartment, apically and basolaterally internalized membrane constituents are thought to be sorted for recycling back to their site of origin or for transcytosis to the opposite plasma membrane domain. We report here that in the epithelial cell line Madin–Darby Canine Kidney (MDCK), antibodies to Rab11a label an apical pericentriolar endosomal compartment that is dependent on intact microtubules for its integrity. Furthermore, this compartment is accessible to a membrane-bound marker (dimeric immunoglobulin A [IgA]) internalized from either the apical or basolateral pole, functionally defining it as the apical recycling endosome. We have also examined the role of a closely related epithelial-specific Rab, Rab25, in the regulation of membrane recycling and transcytosis in MDCK cells. When cDNA encoding Rab25 was transfected into MDCK cells, the protein colocalized with Rab11a in subapical vesicles. Rab25 transfection also altered the distribution of Rab11a, causing the coalescence of immunoreactivity into multiple denser vesicular structures not associated with the centrosome. Nevertheless, nocodazole still dispersed these vesicles, and dimeric IgA internalized from either the apical or basolateral membrane was detected in endosomes labeled with antibodies to both Rab11a and Rab25. Overexpression of Rab25 decreased the rate of IgA transcytosis and of apical, but not basolateral, recycling of internalized ligand. Conversely, expression of the dominant-negative Rab25T26N did not alter either apical recycling or transcytosis. These results indicate that both Rab11a and Rab25 associate with the apical recycling system of epithelial cells and suggest that Rab25 may selectively regulate the apical recycling and/or transcytotic pathways.

scholarly journals A Ypt32p Exchange Factor Is a Putative Effector of Ypt1p

2002 ◽  
Vol 13 (9) ◽  
pp. 3336-3343 ◽  
Author(s):  
Wei Wang ◽  
Susan Ferro-Novick
Keyword(s):  
Secretory Pathway ◽  
Binding Proteins ◽  
Functional Relationship ◽  
Membrane Traffic ◽  
Genetic Studies ◽  
Vesicle Tethering ◽  
Gtp Binding Proteins ◽  
Exchange Factor ◽  
Gtp Binding ◽  
Signal Cascade

Ypt1p regulates vesicle tethering and fusion events from the ER to the Golgi and through the early Golgi. Genetic studies have suggested a functional relationship between Ypt1p and Ypt31p/Ypt32p. Ypt31p and Ypt32p are a pair of functionally redundant GTPases that act after Ypt1p to mediate intra-Golgi traffic or the budding of post-Golgi vesicles from the trans-Golgi. Here we report that a novel Ypt32p exchange factor is a putative effector of Ypt1p. These findings implicate small GTP-binding proteins of the Ypt/Rab family in a signal cascade that directs membrane traffic through the secretory pathway.

scholarly journals Association of the Rho family small GTP-binding proteins with Rho GDP dissociation inhibitor (Rho GDI) in Saccharomyces cerevisiae

Oncogene ◽  
1997 ◽  
Vol 15 (4) ◽  
pp. 417-422 ◽  
Author(s):  
Gertrude Koch ◽  
Kazuma Tanaka ◽  
Tadayuki Masuda ◽  
Wataru Yamochi ◽  
Hidetaro Nonaka ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Binding Proteins ◽  
Gtp Binding Proteins ◽  
Gtp Binding ◽  
Rho Family ◽  
Gdp Dissociation Inhibitor
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