Compartmentalization of rab Proteins in Mammalian Cells

Olkkonen, Vesa M.; Dupree, Paul; Huber, L; Lütcke, Anne; Simons, Kai

doi:10.1007/978-3-642-78267-1_28

Cited by 17 publications

(22 citation statements)

References 109 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Rab5b and Rab5c cDNAs were also cloned in the pGEM-myc plasmid [28] that carries 13 amino acids containing the myc epitope recognized by the 9El0 monoclonal antibodies [26]. The Rab5a Ile ~-~3 mutant was constructed as preciously described [20].…”

Section: Plasmid Constructionmentioning

confidence: 99%

Co‐operative regulation of endocytosis by three RAB5 isoforms

et al. 1995

View full text Add to dashboard Cite

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.

show abstract

Section: Plasmid Constructionmentioning

confidence: 99%

Co‐operative regulation of endocytosis by three RAB5 isoforms

et al. 1995

View full text Add to dashboard Cite

show abstract

“…Subsequent studies identified GS27/membrin (23,24), rbet1 and rsec22b (24,25), GS32 (26), syntaxin 5 (27), syntaxin 6 (28), syntaxin 10 (29), and syntaxin 16 (30,31) as additional Golgi SNAREs. Rab family proteins such as Rab6 (32), Rab10 (33), and Rab12 (34) have been localized to the Golgi complex. Rab6 has been shown to be involved in intra-Golgi protein transport (35,36) and retrograde transport to the endoplasmic reticulum (37).…”

mentioning

confidence: 99%

Sequential Involvement of p115, SNAREs, and Rab Proteins in Intra-Golgi Protein Transport

Gmachl

Wimmer²

2001

Journal of Biological Chemistry

View full text Add to dashboard Cite

Delivery of transport vesicles to their receptor compartment involves tethering, priming, and fusion. Soluble NSF attachment protein-␣ (␣SNAP) mediates the disruption of SNAREs by N-ethylmaleimide sensitive factor (NSF) and was employed to determine the hierarchy of proteins responsible for intra-Golgi protein transport. The N-terminal 23 amino acids of ␣SNAP are necessary for SNARE binding. The antibody 2F10 recognizes this SNARE interaction domain of ␣SNAP and inhibits intraGolgi protein transport reversibly. This antibody was applied to modify the transport assay to determine the protein requirements relative to the action of ␣SNAP and NSF. We found that 1) p115 acts independently of ␣SNAP and NSF, 2) SNAREs are required after tethering and interact selectively after activation by ␣SNAP and NSF, and 3) Rab proteins act after SNARE activation and before fusion.

show abstract

“…Recent studies have localized more than one Rab in the same vesicular carriers and related intracellular compartments (28,29), suggesting that multiple Rabs may associate with vesicular carriers operating at the same relay. If multiple Rabs are present on a single class of transport vesicles, are the sets of Rabs relay-specific or is there overlap?…”

mentioning

confidence: 99%

Rab1a and Multiple Other Rab Proteins Are Associated with the Transcytotic Pathway in Rat Liver

Jin

Saucan

Farquhar

et al. 1996

Journal of Biological Chemistry

View full text Add to dashboard Cite

To better understand the function of Rab1a, we have immunoisolated Rab1a-associated transport vesicles from rat liver using affinity-purified anti-Rab1a-coated magnetic beads. A fraction enriched in endoplasmic reticulum (ER) to Golgi transport vesicles (CV2, ‫؍‬ 1.158) was subjected to immunoisolation, and proteins of the bound and non-bound subfractions were analyzed by Western blotting. To our surprise, we found that immunoisolated vesicles contained not only ER markers (105-kDa form of the polymeric IgA receptor (pIgAR)) but also transcytotic markers (dIgA and the 120-kDa form of pIgAR), suggesting that Rab1a is associated with transcytotic vesicles in rat liver. To investigate this possibility, we used an antibody to the cytoplasmic domain of pIgAR to immunoisolate transcytotic vesicles from a fraction (CV1, ‫؍‬ 1.146) known to be enriched in these vesicles. Rab1a was detected in the immunoadsorbed subfractions. The composition of the vesicles immunoisolated from the CV1 fraction on anti-Rab1a was similar to that of transcytotic vesicles immunoisolated from the same fraction on pIgAR. Both were enriched in transcytotic markers and depleted in ER and Golgi markers. The main difference between the two was that those isolated on anti-Rab1a appeared to be enriched in postendosomal transcytotic vesicles, whereas those isolated on pIgAR contained both pre-and postendosomal elements. Analysis of anti-Rab1a isolated vesicles using [␣-32 P]GTP overlay demonstrated the presence of multiple GTP-binding proteins. Some of these were identified by immunoblotting as epithelia-specific Rab17 and ubiquitous Rabs1b, -2, and -6. Taken together, these results indicate that: 1) Rab1a is associated with both ER to Golgi and postendosomal transcytotic vesicles, and 2) multiple GTP-binding proteins are associated with each class of isolated vesicle.

show abstract

Compartmentalization of rab Proteins in Mammalian Cells

Cited by 17 publications

References 109 publications

Co‐operative regulation of endocytosis by three RAB5 isoforms

Co‐operative regulation of endocytosis by three RAB5 isoforms

Sequential Involvement of p115, SNAREs, and Rab Proteins in Intra-Golgi Protein Transport

Rab1a and Multiple Other Rab Proteins Are Associated with the Transcytotic Pathway in Rat Liver

Contact Info

Product

Resources

About