Phosphorylation of synaptic GTPase-activating protein (synGAP) by Ca2+/calmodulin-dependent protein kinase II (CaMKII) and cyclin-dependent kinase 5 (CDK5) alters the ratio of its GAP activity toward Ras and Rap GTPases (Q35103953)

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English	Phosphorylation of synaptic GTPase-activating protein (synGAP) by Ca2+/calmodulin-dependent protein kinase II (CaMKII) and cyclin-dependent kinase 5 (CDK5) alters the ratio of its GAP activity toward Ras and Rap GTPases	scientific article

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scholarly article

1 reference

Europe PubMed Central

6 August 2017

Phosphorylation of synaptic GTPase-activating protein (synGAP) by Ca2+/calmodulin-dependent protein kinase II (CaMKII) and cyclin-dependent kinase 5 (CDK5) alters the ratio of its GAP activity toward Ras and Rap GTPases (English)

1 reference

Europe PubMed Central

6 August 2017

phosphorylation

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based on heuristic

inferred from title

6

object named as

Sonja Hess

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Europe PubMed Central

6 August 2017

author name string

Ward G Walkup

1

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Europe PubMed Central

6 August 2017

Lorraine Washburn

2

1 reference

Europe PubMed Central

6 August 2017

Michael J Sweredoski

3

1 reference

Europe PubMed Central

6 August 2017

Holly J Carlisle

4

1 reference

Europe PubMed Central

6 August 2017

Robert L Graham

5

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Europe PubMed Central

6 August 2017

Mary B Kennedy

7

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Europe PubMed Central

6 August 2017

language of work or name

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publication date

22 December 2014

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Europe PubMed Central

6 August 2017

Journal of Biological Chemistry

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Europe PubMed Central

6 August 2017

290

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Europe PubMed Central

6 August 2017

4908-4927

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Europe PubMed Central

6 August 2017

8

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Europe PubMed Central

6 August 2017

describes a project that uses

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Europe PubMed Central

11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC4335230/fullTextXML

based on heuristic

inferred from PubMed Central ID database lookup

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The C2 domain of SynGAP is essential for stimulation of the Rap GTPase reaction

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GAP1 family members constitute bifunctional Ras and Rap GTPase-activating proteins

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SynGAP regulates spine formation

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SynGAP-MUPP1-CaMKII synaptic complexes regulate p38 MAP kinase activity and NMDA receptor-dependent synaptic AMPA receptor potentiation

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Regulation of the neuron-specific Ras GTPase-activating protein, synGAP, by Ca2+/calmodulin-dependent protein kinase II

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The NMDA receptor is coupled to the ERK pathway by a direct interaction between NR2B and RasGRF1.

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The role of synaptic GTPase-activating protein in neuronal development and synaptic plasticity

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SynGAP regulates ERK/MAPK signaling, synaptic plasticity, and learning in the complex with postsynaptic density 95 and NMDA receptor

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The cyclin-dependent kinase 5 activators p35 and p39 interact with the alpha-subunit of Ca2+/calmodulin-dependent protein kinase II and alpha-actinin-1 in a calcium-dependent manner

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A decade of CDK5.

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Signal-processing machines at the postsynaptic density

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A synaptic Ras-GTPase activating protein (p135 SynGAP) inhibited by CaM kinase II

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SynGAP: a synaptic RasGAP that associates with the PSD-95/SAP90 protein family

1 reference

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Identifiers

10.1074/JBC.M114.614420

1 reference

Europe PubMed Central

6 August 2017

1 reference

Europe PubMed Central

6 August 2017

1 reference

Europe PubMed Central

6 August 2017

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