RAB5A
RAB5A, member RAS oncogene family
- Ensembl:
- ENSG00000144566
- UniProt:
- P20339
- OMIM:
- 179512
- Synonyms:
- RAB5
Cilia effects upon perturbation of RAB5A
- Cilia number / % ciliated:
- No effect
- Loss-of-function effect:
- No effect
- Overexpression effect:
- No effect
Ciliogenesis screen results (4 screens)
- Kim2016: Not Reported
- Wheway et al. 2015 (siRNA) [siRNA]: No effect PMID:26167766
- Breslow et al. 2018 (CRISPR) [CRISPR]: No Significant Effect PMID:29459680
- Roosing et al. 2015 (siRNA) [siRNA]: No effect PMID:26595381
Phenotypes
- Mouse phenotype:
- increased erythrocyte cell number, increased circulating sodium level, abnormal sleep behavior, decreased grip strength, increased circulating potassium level, decreased mean corpuscular volume, decreased mean corpuscular hemoglobin, decreased circulating hdl cholesterol level
- Mouse ciliopathy phenotype:
- abnormal reti morphology, increased heart weight
Subcellular localization
basal body
Functional category
- Ciliary assembly/disassembly
- Trafficking (BBSome, small GTPases, vesicular transport, ATPases)
- Viral interactions
- Signaling (Hedgehog, GPCRs, ion channels)
- Ciliary membrane
Function
Localisation of the clathrin light chain, AP-2 clathrin adaptor, dynamin and RAB-5 endocytic proteins overlaps with a morphologically discrete periciliary membrane compartment associated with sensory cilia(PMID: 22342749). STAM-1 and RAB-5 collocate in the cell bodies and ciliary bases of polycystin-expressing neurons (Ppkd-2::STAM-1A:: GFP and Ppkd-2::mRFP::RAB-5, Figure 3, B–D). Combined, these data indicate that C. elegans STAM-1A colocalizes with HGRS-1 on the early endosome at the ciliary base, where they may participate in endocytic sorting of LOV-1 and PKD-2(17581863).
Model organism evidence
Systematic proteomic analysis of LRRK2-mediated Rab GTPase phosphorylation establishes a connection to ciliogenesis.
PMIDs: 29125462
How this is achieved is unclear, but protein transport in cilia (intraflagellar transport, IFT) plays an important role.
Transmembrane protein OSTA-1 shapes sensory cilia morphology via regulation of intracellular membrane trafficking in C.