The Rab-GTPase Activating Protein TBC1D1 Regulates Skeletal Muscle
نویسندگان
چکیده
3 Ferenc Szekeres, Alexandra Chadt, Robby Z. Tom, Atul S. Deshmukh, 4 Alexander V. Chibalin, Marie Björnholm, Hadi Al-Hasani and Juleen R. Zierath 5 6 *These authors have contributed equally to this work. 7 8 9 Department of Molecular Medicine and Surgery, Karolinska Institutet, Stockholm, Sweden. 10 German Institute of Human Nutrition, Potsdam-Rehbruecke, Department of Pharmacology, 11 Nuthetal, Germany. Department of Physiology and Pharmacology, Karolinska Institutet, 12 Stockholm, Sweden. 13 14 Running head: TBC1D1 regulates skeletal muscle glucose metabolism. 15 16 Address correspondence to: Professor Juleen R. Zierath, Karolinska Institutet, Section of 17 Integrative Physiology, von Eulers väg 4, 4 Floor, S-171 77 Stockholm, Sweden, Email: 18 [email protected] 19 20 Articles in PresS. Am J Physiol Endocrinol Metab (June 12, 2012). doi:10.1152/ajpendo.00605.2011
منابع مشابه
Insulin-stimulated phosphorylation of the Rab GTPase-activating protein TBC1D1 regulates GLUT4 translocation.
Insulin stimulates the translocation of the glucose transporter GLUT4 from intracellular locations to the plasma membrane in adipose and muscle cells. Prior studies have shown that Akt phosphorylation of the Rab GTPase-activating protein, AS160 (160-kDa Akt substrate; also known as TBC1D4), triggers GLUT4 translocation, most likely by suppressing its Rab GTPase-activating protein activity. Howe...
متن کاملThe Rab-GTPase-activating protein TBC1D1 regulates skeletal muscle glucose metabolism.
The Rab-GTPase-activating protein TBC1D1 has emerged as a novel candidate involved in metabolic regulation. Our aim was to determine whether TBC1D1 is involved in insulin as well as energy-sensing signals controlling skeletal muscle metabolism. TBC1D1-deficient congenic B6.SJL-Nob1.10 (Nob1.10(SJL)) and wild-type littermates were studied. Glucose and insulin tolerance, glucose utilization, hepa...
متن کاملContraction regulates site-specific phosphorylation of TBC1D1 in skeletal muscle
TBC1D1 (tre-2/USP6, BUB2, cdc16 domain family member 1) is a Rab-GAP (GTPase-activating protein) that is highly expressed in skeletal muscle, but little is known about TBC1D1 regulation and function. We studied TBC1D1 phosphorylation on three predicted AMPK (AMP-activated protein kinase) phosphorylation sites (Ser231, Ser660 and Ser700) and one predicted Akt phosphorylation site (Thr590) in con...
متن کاملTBC1D1 Regulates Insulin- and Contraction-Induced Glucose Transport in Mouse Skeletal Muscle
OBJECTIVE TBC1D1 is a member of the TBC1 Rab-GTPase family of proteins and is highly expressed in skeletal muscle. Insulin and contraction increase TBC1D1 phosphorylation on phospho-Akt substrate motifs (PASs), but the function of TBC1D1 in muscle is not known. Genetic linkage analyses show a TBC1D1 R125W missense variant confers risk for severe obesity in humans. The objective of this study wa...
متن کاملDeletion of Both Rab-GTPase-Activating Proteins TBC1D1 and TBC1D4 in Mice Eliminates Insulin- and AICAR-Stimulated Glucose Transport
The Rab-GTPase-activating proteins TBC1D1 and TBC1D4 (AS160) were previously shown to regulate GLUT4 translocation in response to activation of AKT and AMP-dependent kinase. However, knockout mice lacking either Tbc1d1 or Tbc1d4 displayed only partially impaired insulin-stimulated glucose uptake in fat and muscle tissue. The aim of this study was to determine the impact of the combined inactiva...
متن کامل“Deletion of both Rab-GTPase–activating proteins TBC1D1 and TBC1D4 in mice eliminates insulin- and AICAR-stimulated glucose transport [corrected].
The Rab-GTPase–activating proteins TBC1D1 and TBC1D4 (AS160) were previously shown to regulate GLUT4 translocation in response to activation of AKT and AMP-dependent kinase [corrected]. However, knockout mice lacking either Tbc1d1 or Tbc1d4 displayed only partially impaired insulin-stimulated glucose uptake in fat and muscle tissue. The aim of this study was to determine the impact of the combi...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
دوره شماره
صفحات -
تاریخ انتشار 2012