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Dynamin domains

Growth-Arrest-Specific protein 2 Domain Gastrin/cholecystokinin/caerulein family Dynamin GTPase effector domain Gelsolin homology domain G protein y subunit-like motifs Glycoprotein hormone a chain homologs... [Pg.197]

Damke, H., Binns, D. D., Ueda, H., Schmid, S. L., and Baba, T. (2001) Dynamin GTPase domain mutants block endocytic vesicle formation at morphologically distinct stages. Mol Biol Cell 12,2578-2589. [Pg.112]

The pleckstrin-homology domain is named after pleckstrin, where it was found first (pleckstrin is a major platelet protein which is a substrate of protein kinase Pleckstrin and brain spectrin contain two domains, 2 about 120 residues each, with similar sequences in their amino- and carboxy-terminal parts. To date, at least 90 such PH-domain sequences have been described in proteins with very diverse functions, such as spectrin,43 cytosolic protein kinases, phospholipase C isoforms (PLC-P, -y, and the GTPase dynamin,44.45 guanine nucleotide exchange factors for monomeric GTP-bind-ing proteins, the GTPase-acdvating protein for Ras, the Ras-GAP, and cytoskeletal and several other proteins. [Pg.35]

D. Timm, K. Salim, I Gout, 1— Guruprasad, M. Waterfield, and T. Blundell. Crystal structure of the pleckstrin homology domain from dynamin. Nature Struct Biol, 1 (11), 782 788, 1994. [Pg.53]

Dynamin is a microtubule-associated GTP-binding protein. Dynamins are activated by proteinkinase C. They have a PH, a pleckstrin-homology domain and bind inositol phospholipids which aaivate the GTPase of dynamin. Dynamins are involved in microtubule assembly and vesicular traffic. [Pg.309]

Shupliakov O, Low P Grabs D, Gad H, Chen H, David C, Takei K, De Camilli P, Brodin L (1997a) Synaptic vesicle endocytosis impaired by disruption of dynamin-SH3 domain interactions. Science 276 259-263. [Pg.288]

This value refers to the affinity of the SH3 domain for the entire proline-rich region of dynamin. [Pg.227]

Dong, J., Misselwitz, R., Welfle, H., and Westermann, P. (2000). Expression and purification of dynamin II domains and initial studies on structure and function. Protein Expr. Purif. 20, 314-323. [Pg.256]

Grabs, D., Slepnev, V I., Songyang, Z., David, G., Lynch, M., Cantley, L. C., and De Camilli, P. (1997). The SHS domain of amphiphysin binds the proline-rich domain of dynamin at a single site that defines a new SHS binding consensus sequence. /. Biol. Chem. 272, 13419-13425. [Pg.258]

Vidal, M., Goudreau, N., Cornille, E, Cussac, D., Gincel, E., and Garbay, C. (1999). Molecular and cellular analysis of Grb2 SH3 domain mutants Interaction with Sos and dynamin.y. Mol. Biol. 290, 717-730. [Pg.260]

Okamoto, P. M., Herskovits, J. S., and Vallee, R. B. (1997). Role of the basic, proline-rich region of dynamin in Sre homology 3 domain binding and endocytosis. J. Biol. Chem. 272, 11629-11635. [Pg.265]

Dynamin 1, a member of the dynamin family of large GTPases. Mammalian dynamin 1 forms ring-like assemblies aroimd the necks of budding synaptic vesicles. StmeturaUy, it can be subdivided into five domains. The high-resolution X-ray structure of the GTPase domain from Rattus norvegicus was described in 2005 [K. Takei et al.. Nature 1995, 374,186 ... [Pg.112]

Skare P, Kreivi JP, Bergstrom A, Karlsson R (2003) Profilin I colocalizes with speckles and Cajal bodies a possible role in pre-mRNA splicing. Exp Cell Res 286 12-21 Solomaha E, Szeto FL, Yousef MA, Palfrey HC (2005) Kinetics of Src homology 3 domain association with the proline-rich domain of dynamins specificity, occlusion, and the effects of phosphorylation. J Biol Chem 280 23147-23156... [Pg.148]


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See also in sourсe #XX -- [ Pg.528 ]




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