Alternative titles; symbols
HGNC Approved Gene Symbol: GDI2
Cytogenetic location: 10p15.1 Genomic coordinates (GRCh38): 10:5,765,223-5,813,434 (from NCBI)
GDI-beta (GDI2) is a member of the GDP-dissociation inhibitor family, which includes GDI-alpha (GDI1; 300104). The rab GDIs modulate the activity of G proteins of the rab family and play a role in the regulation of vesicle-mediated cellular transport (summary by Sedlacek et al., 1998).
Shisheva et al. (1994) cloned mouse RABGDIB (which they referred to as 'smg p25A GDI') and reported the sequence. Sedlacek et al. (1994) found that the human RABGDIB sequence is 86.5% similar to RABGDIA, which they referred to as 'XAP-4.' Bachner et al. (1995) studied expression patterns of the 2 human genes. They showed that the 2.5-kb mRNA for RABGDIB is ubiquitously expressed, in contrast to RABGDIA, which is expressed primarily in neural and sensory tissues.
Rak et al. (2003) used a combination of chemical synthesis and protein engineering to generate and crystallize the monoprenylated YPT1-RABGDI complex. The structure of this complex was determined to 1.5-angstrom resolution and provided a structural basis for the ability of RABGDI to inhibit nucleotide release by RAB proteins. Isoprenoid binding requires a conformational change that opens a cavity in the hydrophobic core of its domain II. Analysis of the structure provided a molecular basis for understanding a RABGDI mutant that causes mental retardation.
The GDI-beta gene contains 11 exons (Sedlacek et al., 1998).
By in situ hybridization, Sedlacek et al. (1998) demonstrated that the GDI2 gene maps to 10p15; a processed pseudogene maps to 7p13-p11.
Bachner, D., Sedlacek, Z., Korn, B., Hameister, H., Poustka, A. Expression patterns of two human genes coding for different rab GDP-dissociation inhibitors (GDIs), extremely conserved proteins involved in cellular transport. Hum. Molec. Genet. 4: 701-708, 1995. [PubMed: 7543319] [Full Text: https://doi.org/10.1093/hmg/4.4.701]
Rak, A., Pylypenko, O., Durek, T., Watzke, A., Kushnir, S., Brunsveld, L., Waldmann, H., Goody, R. S., Alexandrov, K. Structure of Rab GDP-dissociation inhibitor in complex with prenylated YPT1 GTPase. Science 302: 646-650, 2003. [PubMed: 14576435] [Full Text: https://doi.org/10.1126/science.1087761]
Sedlacek, Z., Konecki, D. S., Korn, B., Klauck, S. M., Poustka, A. Evolutionary conservation and genomic organization of XAP-4, an Xq28 located gene coding for a human rab GDP-dissociation inhibitor (GDI). Mammalian Genome 5: 633-639, 1994. [PubMed: 7849400] [Full Text: https://doi.org/10.1007/BF00411459]
Sedlacek, Z., Munstermann, E., Mincheva, A., Lichter, P., Poustka, A. The human rab GDI beta gene with long retroposon-rich introns maps to 10p15 and its pseudogene to 7p11-p13. Mammalian Genome 9: 78-80, 1998. [PubMed: 9434952] [Full Text: https://doi.org/10.1007/s003359900685]
Shisheva, A., Sudhof, T. C., Czech, M. P. Cloning, characterization, and expression of a novel GDP dissociation inhibitor isoform from skeletal muscle. Molec. Cell. Biol. 14: 3459-3468, 1994. [PubMed: 7513052] [Full Text: https://doi.org/10.1128/mcb.14.5.3459-3468.1994]