Nuclear Sequestration of β-Subunits by Rad and Rem is Controlled by 14-3-3 and Calmodulin and Reveals a Novel Mechanism for Ca2+ Channel Regulation
- 6 January 2006
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 355 (1) , 34-46
- https://doi.org/10.1016/j.jmb.2005.10.013
Abstract
No abstract availableKeywords
This publication has 36 references indexed in Scilit:
- Regulation of L-type Ca2+ Channel Activity and Insulin Secretion by the Rem2 GTPasePublished by Elsevier ,2005
- 14-3-3 and calmodulin control subcellular distribution of Kir/Gem and its regulation of cell shape and calcium channel activityJournal of Cell Science, 2005
- Phosphorylation of Critical Serine Residues in Gem Separates Cytoskeletal Reorganization from Down-Regulation of Calcium Channel ActivityMolecular and Cellular Biology, 2004
- The Dimeric Versus Monomeric Status of 14-3-3ζ Is Controlled by Phosphorylation of Ser58 at the Dimer InterfaceJournal of Biological Chemistry, 2003
- The Ras-like GTPase Gem is involved in cell shape remodelling and interacts with the novel kinesin-like protein KIF9The EMBO Journal, 2001
- The Gem GTP-binding protein promotes morphological differentiation in neuroblastomaOncogene, 2001
- Mechanisms of modulation of voltage‐dependent calcium channels by G proteinsThe Journal of Physiology, 1998
- Calmodulin Binds to and Inhibits GTP Binding of the Ras-like GTPase Kir/GemJournal of Biological Chemistry, 1996
- Rad, a Novel Ras-related GTPase, Interacts with Skeletal Muscle β-TropomyosinPublished by Elsevier ,1996
- Gem: an Induced, Immediate Early Protein Belonging to the Ras FamilyScience, 1994