Neuron
ArticleLocalization and characterization of the binding site for the regulatory subunit of type II cAMP-dependent protein kinase on MAP2
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Cited by (120)
Chemical Genetic Identification of PKC Epsilon Substrates in Mouse Brain
2023, Molecular and Cellular ProteomicsSpecific phosphorylation of microtubule-associated protein 2c by extracellular signal–regulated kinase reduces interactions at its Pro-rich regions
2022, Journal of Biological ChemistryCitation Excerpt :Despite its disordered nature, MAP2c was identified as one of the AKAPs. Residues 80 to 120 in the N-terminal domain of MAP2c bind RIIα-PKA (54) and phosphorylation of Ser136 has been suggested to interfere with its binding (36). Our direct monitoring of RIIα-PKA binding to MAP2c revealed that RIIα-PKA is indeed recognized by residues 80 to 120 of MAP2c, but motions of many residues throughout the whole MAP2c sequence are restricted when the complex is formed (blue circles in Fig. 4A).
Changes in microtubule turnover accompany synaptic plasticity and memory formation in response to contextual fear conditioning in mice
2010, NeuroscienceCitation Excerpt :These include a high level of assembly and dependence of MAP2-associated MTs on signaling via the cAMP/PKA pathway. Interestingly, the regulatory subunit of the PKA has been reported to bind to the amino termini of the MAP2 isoforms (Rubino et al., 1989). Thus newly assembled MAP2-associated MTs might stimulate further recruitment of PKA as part of memory formation; conversely, cAMP might promote the growth of MAP2-associated MTs through activation of locally recruited PKA.
Selectivity in enrichment of cAMP-dependent protein kinase regulatory subunits type I and type II and their interactors using modified cAMP affinity resins
2009, Molecular and Cellular ProteomicsCitation Excerpt :The PKA isoforms, RIIα and RIIβ (white bars on the left) show a log 2 ratio of 3.2 (stdev = 0.12) and 3.9 (stdev = 0.17) whereas RIα and RIβ have similar log 2 ratios of −0.79 (stdev = 0.20) and −0.89 (stdev = 0.16), respectively. Furthermore, 6 AKAPs have similar ratios compared with the RII isoforms:AKAP5, AKAP7, AKAP9, AKAP11, MAP2, and AKAP14 (dark gray bars), indicating they are RII specific AKAPs, in agreement with literature data for AKAP5 (25), AKAP7 (26), AKAP11 (27), and MAP2 (28). On the other hand, AKAP1 (light gray bars) had average ratios of around one indicating that it has similar binding affinities to both RI and RII, so it can be classified as dual specificity AKAP.
Subcellular Targeting of PKA through AKAPs: Conserved Anchoring and Unique Targeting Domains
2009, Handbook of Cell Signaling, Second EditionInteraction of microtubule-associated protein-2 and p63: A new link between microtubules and rough endoplasmic reticulum membranes in neurons
2005, Journal of Biological Chemistry
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Present Address: Department of Biochemical Genetics and Metabolism, Rockefeller University, New York, New York 10021.