The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

GDI2  -  GDP dissociation inhibitor 2

Homo sapiens

Synonyms: GDI-2, Guanosine diphosphate dissociation inhibitor 2, HEL-S-46e, RABGDIB, Rab GDI beta, ...
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of GDI2

 

High impact information on GDI2

 

Biological context of GDI2

  • The human rab GDI beta gene with long retroposon-rich introns maps to 10p15 and its pseudogene to 7p11-p13 [4].
  • To further test whether the endogenous GDI-2 can adopt a gain-of-function conformation, we pharmacologically stimulated intact 3T3-L1 adipocytes to induce GDI-2 tyrosine phosphorylation [5].
  • In this study we have addressed a plausible general activity of GDI-2 in supporting Rab membrane release and have analyzed the requirements of sequence-conserved vs variable regions of GDI-2 in these functional interactions [5].
  • Here we report that GDI-2-containing structural elements are concentrated predominantly in the pericentriolar area in interphase CHO-T cells and differentiated 3T3-L1 adipocytes based on colocalization of GDI-2 and the centrosomal marker pericentrin [6].
 

Anatomical context of GDI2

  • Together, these results indicate that (a) GDI-2 displays a general activity to release Rabs from membranes, (b) GDI-2-conserved residues, but not the C-terminal variable region, are essential for this activity, and (c) structural modifications in GDI-2 can enhance its functional activity, directing selective interactions with individual Rabs [5].
  • During mitotic resolution of the centrosome into two identifiable foci in CHO-T cells, GDI-2 containing structures remain intact and also resolve into two regions surrounding the centrosome [6].
  • The integrity of pericentriolar GDI-2-binding elements was not disrupted by either brief Triton X-100 extraction or microtubule cytoskeletal disassembly, achieved with nocodazole [6].
  • Expressed c-Myc-tagged GDI-2 in transfected COS-7 cells targets to the same region [6].
 

Associations of GDI2 with chemical compounds

  • Dissociation of pericentriolar GDI-2 from the Golgi markers beta-COP and lectin receptors was apparent upon brefeldin A treatment of 3T3-L1 adipocytes or CHO-T cells [6].
 

Enzymatic interactions of GDI2

  • We found a pronounced increase of the Rab4 soluble form and its soluble complexes with the tyrosine-phosphorylated GDI-2 [5].
 

Analytical, diagnostic and therapeutic context of GDI2

  • Localization of both GDI-2 and GLUT4 in the same perinuclear regions of these cells was established by immunofluorescence microscopy, whereas GDI-1 displayed a diffuse, cytoplasmic distribution [2].

References

 
WikiGenes - Universities