Literature DB >> 1765166

MAP2: a sensitive cross-linker and adjustable spacer in dendritic architecture.

P Friedrich1, A Aszódi.   

Abstract

Microtubule-associated protein 2 (MAP2), a long, filamentous molecule thought to cross-link dendritic cytoskeleton, is rich in PEST sequences, putative signals for rapid proteolytic degradation. It is suggested that MAP2 is indeed highly susceptible to protease, e.g. calpain, attack, which is needed for a plastic change, but actual breakdown depends on the regulation of protease(s). Phosphorylation is expected to make the molecule longer and rigid, similarly to what was observed with the related tau protein. Such a structural transition may provide a mechanism for the putative role of MAP2 in dendritic branching.

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Year:  1991        PMID: 1765166     DOI: 10.1016/0014-5793(91)81371-e

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  15 in total

Review 1.  Calpain and synaptic function.

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Review 3.  Making sense of the multiple MAP-2 transcripts and their role in the neuron.

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4.  Dysfunction of microtubule-associated proteins of MAP2/tau family in Prion disease.

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Review 6.  A-kinase anchoring proteins: a key to selective activation of cAMP-responsive events?

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7.  Effect of melatonin on beta-tubulin and MAP2 expression in NIE-115 cells.

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Journal:  Neurochem Res       Date:  1996-06       Impact factor: 3.996

Review 8.  Intrinsic disorder in scaffold proteins: getting more from less.

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9.  Removal of the projection domain of microtubule-associated protein 2 alters its interaction with tubulin.

Authors:  A Fellous; V Prasad; R Ohayon; M A Jordan; R F Ludueña
Journal:  J Protein Chem       Date:  1994-05

10.  Vav3-deficient mice exhibit a transient delay in cerebellar development.

Authors:  Celia Quevedo; Vincent Sauzeau; Mauricio Menacho-Márquez; Antonio Castro-Castro; Xosé R Bustelo
Journal:  Mol Biol Cell       Date:  2010-01-20       Impact factor: 4.138

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