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

Chavrier, Philippe; Vingron, M; Sander, C; Simons, Kai; Zerial, Marino

doi:10.1128/mcb.10.12.6578

Cited by 198 publications

(121 citation statements)

References 33 publications

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“…A small arrow indicates the trypsin cleavage site of E.coli rab5, as determined by N-terminal sequencing of the band recovered from the gel shown in Figure 3, (Padfield et al, 1992). This peptide was selected as a control, because, when compared with most other monomeric GTP-binding proteins (Chavrier et al, 1990b;Valencia et al, 1991), both rab3 and rab5 contain relatively long N-terminal extensions forming an additional domain (see Figure 6). As shown in Figure 7, fusion was inhibited in our assay by relatively low concentrations of the rab5 N-terminal peptide under conditons where the rab3b N-terminal peptide or a rab2 Cterminal peptide were without effect.…”

Section: Rab5 Associated With Early Endosomal Membranes Is Trypsin-sementioning

confidence: 99%

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The N-terminal domain of a rab protein is involved in membrane-membrane recognition and/or fusion.

et al. 1994

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Proteins of the YPT1/SEC4/rab family are well documented to be involved in the regulation of membrane transport. We have previously reported that rab5 regulates endosome-endosome recognition and/or fusion in vitro. Here, we show that this process depends on the rab5 N-terminal domain. Treatment of early endosomal membranes at a low trypsin concentration essentially abolished fusion and cleaved rab5 to a 1 kDa smaller polypeptide. Two-dimensional gel analysis suggested that rab5 is one of the few, if not the only, polypeptides cleaved by trypsin under these conditions. Whereas endosome fusion could be stimulated by cytosol prepared from cells overexpressing rab5 (and thus containing high amounts of the protein), this stimulation was abolished by trypsin-treatment of the cytosol. Trypsin-treated cytosol prepared from mock-transfected cells, which contains very low amounts of rab5, showed no inhibitory activity indicating that rab5 is the target of trypsin in these experiments. Purified rab5 prepared after expression in Escherichia coli was treated with trypsin, which cleaved the protein at the N-terminus. A synthetic peptide of rab5 N-terminal domain inhibited endosome fusion in our cell-free assay. A version of the same peptide truncated at the N-terminus or a peptide of rab3 N-terminal domain were without effects. Altogether, these observations suggest that the N-terminal domain of rab5 is involved in the process of early endosome recognition and/or fusion, presumably because it interacts with another component of the transport machinery.

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Section: Rab5 Associated With Early Endosomal Membranes Is Trypsin-sementioning

confidence: 99%

“…N-terminal sequence of rab proteins. The N-terminal domains of different rab proteins were aligned according to Chavrier et al (1990b). The sequences of the rab3b and rab5 N-terminal domain peptides are underlined.…”

Section: Rab5 Associated With Early Endosomal Membranes Is Trypsin-sementioning

confidence: 99%

The N-terminal domain of a rab protein is involved in membrane-membrane recognition and/or fusion.

et al. 1994

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“…However, the precise function of rab proteins in this complex process is not yet understood. We have investigated the subcellular distribution of rabllp [5], which although ubiquitously expressed, has been reported to be more abundant in tissues with a high level of secretion [6]. This observation suggested that rabl lp might play a role in the exocytic pathway.…”

Section: Introductionmentioning

confidence: 99%

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

et al. 1993

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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.

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“…Therefore, this subgroup of closely related proteins seems to be quite heterogeneous, its members having a cell type specific localization and possibly different functions. For Rab4 two isoforms have been discovered: Rab4a is present on the early endosome and regulate recycling but the localization and the function of Rab4b are not yet known [15][16][17].…”

Section: Introductionmentioning

confidence: 99%

Co‐operative regulation of endocytosis by three RAB5 isoforms

et al. 1995

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Rab proteins are small GTPases involved in the regulation of membrane traffic. Rab5a has been shown to regulate transport in the early endocytic pathway. Here we report the isolation of cDNA clones encoding two highly related isoforms, Rab5b and Rab5c. The two proteins share with Rab5a all the structural features required for regulation of endocytosis. Rab5b and Rab5c colocalize with the both transferrin receptor and Rab5a, stimulate the homotypic fusion between early endosomes in vitro and increase the rate of endocytosis when overexpressed in vivo. These data demonstrate that three Rab5 isoforms cooperate in the regulation of endocytosis in eukaryotic cells.

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

Cited by 198 publications

References 33 publications

The N-terminal domain of a rab protein is involved in membrane-membrane recognition and/or fusion.

The N-terminal domain of a rab protein is involved in membrane-membrane recognition and/or fusion.

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

Co‐operative regulation of endocytosis by three RAB5 isoforms

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