Hsp90 Interactions and Acylation Target the G Protein Gα12 but Not Gα13 to Lipid Rafts
Open Access
- 1 September 2002
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 277 (36) , 32409-32412
- https://doi.org/10.1074/jbc.c200383200
Abstract
No abstract availableKeywords
This publication has 39 references indexed in Scilit:
- Interaction between the Gα Subunit of Heterotrimeric G12 Protein and Hsp90 Is Required for Gα12 SignalingPublished by Elsevier ,2001
- AKAP-Lbc Anchors Protein Kinase A and Nucleates Gα12-selective Rho-mediated Stress Fiber FormationJournal of Biological Chemistry, 2001
- Hsp90: Chaperoning signal transductionJournal of Cellular Physiology, 2001
- In vivo functions of heterotrimeric G-proteins: studies in Gα-deficient miceOncogene, 2001
- Interaction of Galpha 12 and Galpha 13 with the cytoplasmic domain of cadherin provides a mechanism for beta -catenin releaseProceedings of the National Academy of Sciences, 2001
- Acylation of Gα13is important for its interaction with thrombin receptor, transforming activity and actin stress fiber formationFEBS Letters, 2000
- Direct Stimulation of the Guanine Nucleotide Exchange Activity of p115 RhoGEF by Gα 13Science, 1998
- A cysteine‐11 to serine mutant of Gα12 impairs activation through the thrombin receptorFEBS Letters, 1998
- Gα12 Requires Acylation for Its Transforming ActivityBiochemistry, 1998
- Constitutively Active Gαq and Gα13 Trigger Apoptosis through Different PathwaysPublished by Elsevier ,1997