Disease relevance of Rab11a

• These data identify Rab11a as a novel, tumor-associated c-Fos/AP-1 target and may point to an as yet unrecognized function of Rab11a in the development of skin cancer [1].
• Mouse polyomavirus enters early endosomes, requires their acidic pH for productive infection, and meets transferrin cargo in Rab11-positive endosomes [2].

High impact information on Rab11a

• Expression of Rab11 25N, a GTP binding-deficient allele of Rab11, led to a decreased rate of transferrin efflux and impaired Fc(gamma)R-mediated phagocytosis, where Fc(gamma)R is the receptor for the Fc portion of IgG [3].
• Macrophages expressing epitope-tagged Rab11 demonstrated the presence of Rab11 in several intracellular membrane compartments, including endosomes and nascent phagosomes [3].
• A Rab11-containing rapidly recycling compartment in macrophages that promotes phagocytosis [3].
• 72-5ptase expression promoted GLUT4 trafficking via a Rab11-dependent pathway but not by Rab5-mediated endocytosis [4].
• Moreover, dexamethasone, which is a potent inhibitor of AP-1-mediated transactivation that exhibits anti-inflammatory and anti-tumor promoting activities, inhibited TPA-induced expression of Rab11a [1].

Biological context of Rab11a

• The Rab11a and Rab25 genes are localized to chromosomes 9C and 3E3/F1, respectively [5].
• Thus, while Rab11a and Rab11b share high sequence homology, they appear to reside within distinct vesicle compartments [6].
• To monitor further trafficking of PyV, we used fluorescent resonance energy transfer (FRET) to determine mutual localization of PyV VP1 with transferrin and Rab11 GTPase at a 2- to 10-nm resolution [2].

Anatomical context of Rab11a

• In rabbit gastric parietal cells, unlike Rab11a, Rab11b did not colocalize or coisolate with H(+)/K(+)-ATPase [6].
• Rab11b resides in a vesicular compartment distinct from Rab11a in parietal cells and other epithelial cells [6].
• These results indicate that in contrast to Rab11a, the Rab11b compartment in the apical region is not as dependent upon microtubules [6].
• Within the Rab11a gene promoter, we identified a functional AP-1 binding element that exhibited elevated c-Fos binding activity after TPA treatment of keratinocytes [1].
• Rab11-FIP2 is a member of a newly identified family of Rab11-binding proteins that have been implicated in the function of recycling endosomes [7].

Co-localisations of Rab11a

• In contrast, Rab11 colocalized with V-ATPase in apical regions of proximal tubule, and Rab20 colocalized with the enzyme in intercalated cells [8].

Regulatory relationships of Rab11a

• Knocking out RhoB or expressing a dominant-interfering Rab11 mutant suppresses both catalytic activation of Src and translocation of active kinase to peripheral membrane structures [9].

Other interactions of Rab11a

• While recent work on Rab11a and Rab25 has yielded some insights into their function, Rab11b has received little attention [6].
• Light microscopy and fractionation studies reveal that MR colocalizes predominantly with Rab5a and partially with Rab11, an endosomal recycling pathway marker [10].
• Although we found close apposition between LDs and endosomal compartments labeled by expressed Rab5, Rab7, or Rab11 constructs, there was no detectable labeling of the LD surface itself by these Rab proteins [11].
• ACRP30 is secreted from 3T3-L1 adipocytes via a Rab11-dependent pathway [12].
• Using the antibody, Rab11 p24 was shown to be abundant in rat pancreas as well as in most rat tissues [13].

References