A New Member of the TBC1D15 Family from Chiloscyllium plagiosum: Rab GTPase-Activating Protein Based on Rab7 as a Substrate
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A New Member of the TBC1D15 Family from Chiloscyllium plagiosum: Rab GTPase-Activating Protein Based on Rab7 as a Substrate
APSL (active peptide from shark liver) is a hepatic stimulator cytokine from the liver of Chiloscyllium. It can effectively protect islet cells and improve complications in mice with alloxan-induced diabetes. Here, we demonstrate that the APSL sequence is present in the N-terminus of novel TBC (Tre-2, Bub2 and Cdc16) domain family, member 15 (TBC1D15) from Chiloscyllium plagiosum. This shark TB...
متن کاملTBC domain family, member 15 is a novel mammalian Rab GTPase-activating protein with substrate preference for Rab7.
Ypt/Rabs are Ras-related GTPases that function as key regulators of intracellular vesicular trafficking. Their slow intrinsic rates of GTP hydrolysis are catalyzed by GTPase-activating proteins (GAPs). Ypt/Rab-GAPs constitute a family of proteins that contain a TBC (Tre-2/Bub2/Cdc16) domain. Only three of the 51 family members predicted in the human genome are confirmed Ypt/Rab-GAPs. Here, we r...
متن کاملTwo new members of a family of Ypt/Rab GTPase activating proteins. Promiscuity of substrate recognition.
Monomeric GTPases of the Ras superfamily have a very slow intrinsic GTPase activity which is accelerated by specific GTPase-activating proteins. In contrast to Ras- and Rho-specific GTPase-activating proteins (GAPs) that have been studied in great detail, little is known about the functioning of GAPs specific for Ypt/Rab transport GTPases. We have identified two novel Ypt/Rab-GAPs because of th...
متن کاملRab GTPase-activating protein domain
Cristinel P. MÎINEA*1, Hiroyuki SANO*1, Susan KANE*, Eiko SANO*, Mitsunori FUKUDA†, Johan PERÄNEN‡, William S. LANE§ and Gustav E. LIENHARD*2 *Department of Biochemistry, Dartmouth Medical School, Hanover, NH 03755, U.S.A., †Fukuda Initiative Research Unit, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan, ‡Institute of Biotechnology, Program in Cellular Biotechnology, FIN-00014, University o...
متن کاملSubstrate specificity and effect on GLUT4 translocation of the Rab GTPase-activating protein Tbc1d1.
Insulin stimulation of the trafficking of the glucose transporter GLUT4 to the plasma membrane is controlled in part by the phosphorylation of the Rab GAP (GTPase-activating protein) AS160 (also known as Tbc1d4). Considerable evidence indicates that the phosphorylation of this protein by Akt (protein kinase B) leads to suppression of its GAP activity and results in the elevation of the GTP form...
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ژورنال
عنوان ژورنال: Marine Drugs
سال: 2015
ISSN: 1660-3397
DOI: 10.3390/md13052955