RGD Reference Report - Regulation of synaptojanin 1 by cyclin-dependent kinase 5 at synapses. - Rat Genome Database

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Regulation of synaptojanin 1 by cyclin-dependent kinase 5 at synapses.

Authors: Lee, SY  Wenk, MR  Kim, Y  Nairn, AC  De Camilli, P 
Citation: Lee SY, etal., Proc Natl Acad Sci U S A. 2004 Jan 13;101(2):546-51. Epub 2004 Jan 2.
RGD ID: 2312451
Pubmed: PMID:14704270   (View Abstract at PubMed)
PMCID: PMC327184   (View Article at PubMed Central)
DOI: DOI:10.1073/pnas.0307813100   (Journal Full-text)

Synaptojanin 1 is a polyphosphoinositide phosphatase concentrated in presynaptic nerve terminals, where it dephosphorylates a pool of phosphatidylinositol 4,5-bisphosphate implicated in synaptic vesicle recycling. Like other proteins with a role in endocytosis, synaptojanin 1 undergoes constitutive phosphorylation in resting synapses and stimulation-dependent dephosphorylation by calcineurin. Here, we show that cyclin-dependent kinase 5 (Cdk5) phosphorylates synaptojanin 1 and regulates its function both in vitro and in intact synaptosomes. Cdk5 phosphorylation inhibited the inositol 5-phosphatase activity of synaptojanin 1, whereas dephosphorylation by calcineurin stimulated such activity. The activity of synaptojanin 1 was also stimulated by its interaction with endophilin 1, its major binding partner at the synapse. Notably, Cdk5 phosphorylated serine 1144, which is adjacent to the endophilin binding site. Mutation of serine 1144 to aspartic acid to mimic phosphorylation by Cdk5 inhibited the interaction of synaptojanin 1 with endophilin 1. These results suggest that Cdk5 and calcineurin may have an antagonistic role in the regulation of synaptojanin 1 recruitment and activity, and therefore in the regulation of phosphatidylinositol 4,5-bisphosphate turnover at synapses.

Objects referenced in this article
Gene Synj1 synaptojanin 1 Rattus norvegicus

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