Linked Life Data

10704996

Source:http://linkedlifedata.com/resource/pubmed/id/10704996

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2000-6-19
pubmed:abstractText
Neurons, the basic information processing units of the nervous system, are characterized by a complex polar morphology which is essential for their function. To attain their precise morphology, neurons extend cytoplasmatic processes (axons and dendrites) and establish synaptic connections in a highly regulated way. Additionally, neurons are also subjected to small plastic changes at the adult stage which serve to regulate synaptic transmission. Every step of neuronal development is genetically controlled by endogenous determinants, as well as by environmental signals including intercellular contacts, extracellular matrix and diffusible signals. Cytoskeletal components are among the main protein targets modified in response to most of those extracellular signals which ultimately determine neuronal morphology. One of the major mechanisms controlling the neuronal cytoskeleton is the modification of the phosphorylation state of cytoskeletal proteins via changes in the relative activities of protein kinases and phosphatases within neurons. In particular, the microtubule-associated protein 2 (MAP2) family of proteins is an abundant group of cytoskeletal components which are predominantly expressed in neurons and serve as substrates for most of protein kinases and phosphatases present in neurons. MAP2 phosphorylation seems to control its association with the cytoskeleton and it is developmentally regulated. Moreover, MAP2 may perform many functions including the nucleation and stabilization of microtubules (and maybe microfilaments), the regulation of organelle transport within axons and dendrites, as well as the anchorage of regulatory proteins such as protein kinases which may be important for signal transduction. These putative functions of MAP2 have also been proposed to play important roles in the outgrowth of neuronal processes, synaptic plasticity and neuronal cell death. Thus, MAP2 constitutes an interesting case to understand the regulation of neuronal function by the alteration of the phosphorylation state of cytoskeletal proteins in response to different extracellular signals. Here we will review the current knowledge about the regulation of MAP2 function through phosphorylation/dephosphorylation and its relevance in the broader context of neuronal functions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0301-0082
pubmed:author
pubmed:issnType
Print
pubmed:volume
61
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
133-68
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:10704996-Animals, pubmed-meshheading:10704996-Axonal Transport, pubmed-meshheading:10704996-Axons, pubmed-meshheading:10704996-Brain, pubmed-meshheading:10704996-Cytoskeleton, pubmed-meshheading:10704996-Hippocampus, pubmed-meshheading:10704996-Humans, pubmed-meshheading:10704996-Long-Term Potentiation, pubmed-meshheading:10704996-Microtubule-Associated Proteins, pubmed-meshheading:10704996-Microtubules, pubmed-meshheading:10704996-Morphogenesis, pubmed-meshheading:10704996-Nerve Tissue Proteins, pubmed-meshheading:10704996-Nervous System Diseases, pubmed-meshheading:10704996-Neuronal Plasticity, pubmed-meshheading:10704996-Neurons, pubmed-meshheading:10704996-Neurotoxins, pubmed-meshheading:10704996-Phosphoprotein Phosphatases, pubmed-meshheading:10704996-Phosphorylation, pubmed-meshheading:10704996-Protein Isoforms, pubmed-meshheading:10704996-Protein Kinases, pubmed-meshheading:10704996-Protein Processing, Post-Translational, pubmed-meshheading:10704996-Synapses
pubmed:year
2000
pubmed:articleTitle
Phosphorylation of microtubule-associated protein 2 (MAP2) and its relevance for the regulation of the neuronal cytoskeleton function.
pubmed:affiliation
Centro de Biología Molecular "Severo Ochoa", Facultad de Ciencias, Universidad Autónoma de Madrid (CSIC-UAM), Cantoblanco, 28049, Madrid, Spain. csanchez@cbm.uam.es
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't