cd04124

Rab GTPase-like family 2 (Rab-like2)

CDD entry
Member databaseCDD
CDD typedomain
Short nameRabL2
SetP-loop_NTPase

Description

RabL2 (Rab-like2) subfamily. RabL2s are novel Rab proteins identified recently which display features that are distinct from other Rabs, and have been termed Rab-like. RabL2 contains RabL2a and RabL2b, two very similar Rab proteins that share > 98% sequence identity in humans. RabL2b maps to the subtelomeric region of chromosome 22q13.3 and RabL2a maps to 2q13, a region that suggests it is also a subtelomeric gene. Both genes are believed to be expressed ubiquitously, suggesting that RabL2s are the first example of duplicated genes in human proximal subtelomeric regions that are both expressed actively. Like other Rab-like proteins, RabL2s lack a prenylation site at the C-terminus. 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.
[7, 8, 12, 9, 13, 14, 16, 17, 1, 15, 18, 3, 4, 11, 6, 2, 10, 5, 19]

References

1.Ypt and Rab GTPases: insight into functions through novel interactions. Segev N. Curr. Opin. Cell Biol. 13, 500-11, (2001). View articlePMID: 11454458

2.Rabs, Rips, FIPs, and endocytic membrane traffic. Prekeris R. ScientificWorldJournal 3, 870-80, (2003). View articlePMID: 14532427

3.Multiple aspects of Rab protein action in the secretory pathway: focus on Rab3 and Rab6. Darchen F, Goud B. Biochimie 82, 375-84, (2000). View articlePMID: 10865125

4.How do Rab proteins function in membrane traffic? Armstrong J. Int. J. Biochem. Cell Biol. 32, 303-7, (2000). View articlePMID: 10716627

5.Regulation of membrane transport by rab GTPases. Deneka M, Neeft M, van der Sluijs P. Crit. Rev. Biochem. Mol. Biol. 38, 121-42, (2003). View articlePMID: 12749696

6.Vesicle transport: a close collaboration of Rabs and effectors. Spang A. Curr. Biol. 14, R33-4, (2004). View articlePMID: 14711434

7.Two novel human RAB genes with near identical sequence each map to a telomere-associated region: the subtelomeric region of 22q13.3 and the ancestral telomere band 2q13. Wong AC, Shkolny D, Dorman A, Willingham D, Roe BA, McDermid HE. Genomics 59, 326-34, (1999). View articlePMID: 10444334

8.The Rab GTPase family. Stenmark H, Olkkonen VM. Genome Biol. 2, REVIEWS3007, (2001). View articlePMID: 11387043

9.Rab GTPases, intracellular traffic and disease. Seabra MC, Mules EH, Hume AN. Trends Mol Med 8, 23-30, (2002). View articlePMID: 11796263

10.Rab and ARF GTPase regulation of exocytosis. Collins RN. Mol. Membr. Biol. 20, 105-15, (2003). View articlePMID: 12851068

11.Rab GTPases coordinate endocytosis. Somsel Rodman J, Wandinger-Ness A. J. Cell. Sci. 113 Pt 2, 183-92, (2000). PMID: 10633070

12.Direct interactions between rab GTPases and cargo. Smythe E. Mol. Cell 9, 205-6, (2002). View articlePMID: 11864591

13.Structural clues to Rab GTPase functional diversity. Pfeffer SR. J Biol Chem 280, 15485-8, (2005). PMID: 15746102

14.Rabs grab motors: defining the connections between Rab GTPases and motor proteins. Hammer JA 3rd, Wu XS. Curr. Opin. Cell Biol. 14, 69-75, (2002). View articlePMID: 11792547

15.Rab proteins as membrane organizers. Zerial M, McBride H. Nat. Rev. Mol. Cell Biol. 2, 107-17, (2001). View articlePMID: 11252952

16.Rab GTPases: specifying and deciphering organelle identity and function. Pfeffer SR. Trends Cell Biol. 11, 487-91, (2001). View articlePMID: 11719054

17.Ypt/rab gtpases: regulators of protein trafficking. Segev N. Sci. STKE 2001, re11, (2001). View articlePMID: 11579231

18.Structural basis for Rab function: an overview. Moyer BD, Balch WE. Meth. Enzymol. 329, 3-6, (2001). View articlePMID: 11210547

19.The Arabidopsis Rab GTPase family: another enigma variation. Rutherford S, Moore I. Curr. Opin. Plant Biol. 5, 518-28, (2002). View articlePMID: 12393015

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