Identification of ras-related, YPT family genes in Schizosaccharomyces pombe.

Miyake, Shingo; Yamamoto, Masayuki

doi:10.1002/j.1460-2075.1990.tb08257.x

Cited by 74 publications

(50 citation statements)

References 41 publications

(56 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Rabll is highly homologous to Ypt3p (24) and equivalent to SP8p (11) recently found in S. pombe. Deletion of the YPT3 gene causes a temperature-sensitive lethal phenotype (24), but its intracellular location and function are unknown at present.…”

Section: Discussionmentioning

confidence: 68%

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

Chavrier¹,

Vingron²,

Sander³

et al. 1990

Mol. Cell. Biol.

198

115

View full text Add to dashboard Cite

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.

show abstract

Section: Discussionmentioning

confidence: 68%

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

Chavrier¹,

Vingron²,

Sander³

et al. 1990

Mol. Cell. Biol.

198

115

View full text Add to dashboard Cite

show abstract

“…The presence of rabl lp on both constitutive and regulated secretory pathways and its tissue distribution make it unlikely that the function of rabl lp is involved in a process that is restricted to the regulated secretory pathway. Indeed, the existence of a highly homologous protein in yeast, ypt3 [5,26] suggests that this protein even plays a role in a lower eucaryote for which no regulated secretion has been described so far. Recently it has been postulated that both constitutive and regulated secretion are based on the same principles with the exception of an inhibitory factor, restricted to the regulated secretory pathway and neutralized only in response to an extracellular trigger [27].…”

Section: Discussionmentioning

confidence: 99%

Rab11, a small GTPase associated with both constitutive and regulated secretory pathways in PC12 cells

et al. 1993

View full text Add to dashboard Cite

A specific polyclonal antibody was used to investigate the subcellular distribution of the small GTPase, rabl 1 p, in the neuroendocrine cell line, PC12. We took advantage of a previously described pulse-chase protocol based on sulfation [1] to examine the distribution of rabl 1 along the secretory pathway. Using the rabl 1 antiserum, but not serum depleted of rabl 1 antibodies, we were able to specifically immunoisolate markers of the constitutive and the regulated secretory pathway in the trans-Golgi network (TGN) as well as after their exit from this compartment (constitutive secretory vesicles, immature, and mature secretory granules). We therefore conclude that rabl lp is associated with the TGN and with TGN-derived vesicles of both the constitutive and the regulated secretory pathway in PC12 cells.

show abstract

“…The COOH-terminal region may represent a targeting domain as it is the case for the GTP-binding proteins rabS and rab7 (Chavrier et al, 1991). However, this domain presents a degree of conservation that is much higher than that observed between COOH-terminal domain of functional homologues of the rab family (Haubruck et al, 1990;Hengst et al, 1990;Miyake and Yamamoto, 1990), suggesting that it could be required not only for the targeting of SarIp to the ER membrane but also for another aspect of Sarlp function. Analysis of the in vivo and in vitro effects of mutations in conserved residues of the GTP-binding and (Nakano et al, 1988;d'Enfert et al, 1991a SThI or STL2 complements a secl2ts mutation and a secl2 null mutation, the latter normally being lethal for the cells (Nakano et al, 1988 Nakano et al (1988) only identified the SARI gene as a multi-copy suppressor of the secl2ts mutation.…”

Section: Introductionmentioning

confidence: 99%