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The specific functions of RabL2a and RabL2b remain unknown. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. 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Biol.","authors":["Deneka M","Neeft M","van der Sluijs P."],"DOI_URL":"https://doi.org/10.1080/713609214"},"PUB00087753":{"PMID":11719054,"ISBN":null,"volume":"11","issue":"12","year":2001,"title":"Rab GTPases: specifying and deciphering organelle identity and function.","URL":null,"raw_pages":"487-91","medline_journal":"Trends Cell Biol","ISO_journal":"Trends Cell Biol.","authors":["Pfeffer SR."],"DOI_URL":"https://doi.org/10.1016/S0962-8924(01)02147-X"},"PUB00087757":{"PMID":11210547,"ISBN":null,"volume":"329","issue":null,"year":2001,"title":"Structural basis for Rab function: an overview.","URL":null,"raw_pages":"3-6","medline_journal":"Methods Enzymol","ISO_journal":"Meth. 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