Download Cyclin Dependent Kinase 5 (Cdk5) by Toshio Ohshima (auth.), Li-Huei Tsai, Nancy Y. Ip (eds.) PDF

By Toshio Ohshima (auth.), Li-Huei Tsai, Nancy Y. Ip (eds.)

ISBN-10: 0387788867

ISBN-13: 9780387788869

Cyclin based Kinase 5 offers a accomplished and updated selection of stories at the discovery, signaling mechanisms and services of Cdk5, in addition to the aptitude implication of Cdk5 within the therapy of neurodegenerative illnesses. because the id of this targeted member of the Cdk family members, Cdk5 has emerged as probably the most vital sign transduction mediators within the improvement, upkeep and fine-tuning of neuronal services and networking. additional experiences have published that Cdk5 can be linked to the rules of neuronal survival in the course of improvement in addition to in neurodegenerative ailments. those observations point out that particular keep an eye on of Cdk5 is key for the legislation of neuronal survival. The pivotal position that Cdk5 seems to play in either the law of neuronal survival and synaptic capabilities hence increases the attention-grabbing danger that Cdk5 inhibitors could have healing capability for the remedy of a few neurodegenerative diseases.

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Extra resources for Cyclin Dependent Kinase 5 (Cdk5)

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Sema3A-Induced Growth Cone Collapse Through Phosphorylation of CRMP2, and Evidence for Both CRMP1 and CRMP2 Are Involved in Sema3A Signaling We examined whether Sema3A induced growth cone collapse through phosphorylation of CRMP2 by Cdk5 and GSK3b. Immunoblot analysis using antipS522-CRMP1/2 antibody revealed that Sema3A increased phosphorylation of 18 Y. Goshima et al. endogenous CRMP1 and/or CRMP2 at Ser522 in an olomoucine-sensitive manner. , 2005). These CRMP1 and CRMP2 antibodies recognized both non-phosphorylated and phosphorylated forms of CRMP1 and CRMP2, respectively.

The inhibition of calcineurin can potentiate glutamate release after stimulation, suggesting that phosphorylation at P-sites 4, 5, and 6 by MAPK or Cdk5 facilitates trafficking of synaptic vesicles. Cdk5 and Munc-18 Munc-18 was isolated as a syntaxin-binding protein, which is a mammalian homologue of UNC-18 in C. , 1980). , 1993b). In these mice, synaptic transmission was completely abolished, whereas synaptogenesis was normal and postsynaptic receptors were functional. Since synaptic vesicles could still dock to the presynaptic membrane in Munc-18 knockout mice, the function of Munc-18 in synaptic vesicle release is most likely downstream of docking.

J. Biol. Chem. 275, 11610–11617. C. (1993). Dynamin GTPase regulated by protein kinase C phosphorylation in nerve terminals. Nature 365, 163–166. Y. (2004). GTP-dependent secretion from neutrophils is regulated by Cdk5. J. Biol. Chem. 279, 53932–53936. Y. (2000). Cdk5/p25(nck5a) interaction with synaptic proteins in bovine brain. J. Cell Biochem. 78, 151–159. , and Greengard, P. (1986). Characterization of synapsin I binding to small synaptic vesicles. J. Biol. Chem. 261, 8383–8390. , and Greengard, P.

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