Dynamin GTPase regulated by protein kinase C phosphorylation in nerve terminals (original) (raw)
- Letter
- Published: 09 September 1993
- Jean-Marie Sontag2,3,
- Jun-Ping Liu1,
- Else Marie Fykse2,3,
- Clive Slaughter2,
- Harvey McMahontt2,3 &
- …
- Thomas C. Südhof2,3
Nature volume 365, pages 163–166 (1993)Cite this article
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Abstract
DYNAMIN is a microtubule-binding protein with a microtubule-activated GTPase activity1,3. The gene encoding dynamin is mut-ated in _shibire_4,5, a Drosophila mutant defective in endocytosis in nerve terminals and other cells6–9. These observations place dyna-min into two distinct functional contexts, suggesting roles in microtubule-based motility or in endocytosis. We report here that dynamin is identical to the neuronal phosphoprotein dephosphin (P96), originally identified by its stimulus-dependent dephosphorylation in nerve terminals10–13. Dynamin is a protein doublet of Mr 94 and 96K arising by alternative splicing of its primary transcript. In the nerve terminal, both forms of dynamin are phosphorylated by protein kinase C (PKC) and are quantitatively dephosphoryla-ted on excitation. In vitro, dynamin is also phosphorylated by casein kinase II which inhibits PKC phosphorylation. Phosphory-lation by PKC but not by casein kinase II enhances the GTPase activity of dynamin 12-fold. The dynamins are therefore a group of nerve terminal phosphoproteins whose GTPase is regulated by phosphorylation in parallel with synaptic vesicle recycling. The regulation of dynamin GTPase could serve as the trigger for the rapid endocytosis of synaptic vesicles after exocytosis.
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Authors and Affiliations
- Endocrine Unit, John Hunter Hospital, Locked Bag 1, Hunter Region Mail Centre, Newcastle, New South Wales, 2310, Australia
Phillip J. Robinson & Jun-Ping Liu - Department of Molecular Genetics, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas, 75235, USA
Jean-Marie Sontag, Else Marie Fykse, Clive Slaughter, Harvey McMahontt & Thomas C. Südhof - Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas, 75235, USA
Jean-Marie Sontag, Else Marie Fykse, Harvey McMahontt & Thomas C. Südhof
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Robinson, P., Sontag, JM., Liu, JP. et al. Dynamin GTPase regulated by protein kinase C phosphorylation in nerve terminals.Nature 365, 163–166 (1993). https://doi.org/10.1038/365163a0
- Received: 20 April 1993
- Accepted: 04 June 1993
- Issue Date: 09 September 1993
- DOI: https://doi.org/10.1038/365163a0