Phosphorylation of Dynamin I on Ser-795 by Protein Kinase C Blocks Its Association with Phospholipids
Open Access
- 1 April 2000
- journal article
- Published by Elsevier
- Vol. 275 (16) , 11610-11617
- https://doi.org/10.1074/jbc.275.16.11610
Abstract
No abstract availableKeywords
This publication has 43 references indexed in Scilit:
- The Pleckstrin Homology Domain of Protein Kinase D Interacts Preferentially with the η Isoform of Protein Kinase CJournal of Biological Chemistry, 1999
- Phosphorylation of dynamin by ERK2 inhibits the dynamin‐microtubule interactionFEBS Letters, 1996
- A presynaptic inositol-5-phosphataseNature, 1996
- Molecular Cloning and Characterization of a New Member of the RAC Protein Kinase Family: Association of the Pleckstrin Homology Domain of 3 Types of RAC Protein Kinase with Protein Kinase C Subspecies and βγ Subunits of G ProteinsBiochemical and Biophysical Research Communications, 1995
- Phosphorylation of dynamin I and synaptic-vesicle recyclingTrends in Neurosciences, 1994
- Phosphorylation of Dynamin by CDC2 KinaseBiochemical and Biophysical Research Communications, 1994
- Dephosphin, a 96 000 Da substrate of protein kinase C in synaptosomal cytosol, is phosphorylated in intact synaptosomesFEBS Letters, 1991
- Phosphorylation of synaptosomal cytoplasmic proteins: Inhibition of calcium-activated, phospholipid-dependent protein kinase (protein kinase c) by bay k 8644Neurochemistry International, 1988
- Dephosphorylation of Synaptosomal Proteins P96 and P139 Is Regulated by Both Depolarization and Calcium, but Not by a Rise in Cytosolic Calcium AloneJournal of Neurochemistry, 1987
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970