Protein tyrosine phosphorylation: implications for synaptic function.

Abstract:

:The phosphorylation of proteins on tyrosine residues, initially believed to be primarily involved in cell growth and differentiation, is now recognized as having a critical role in regulating the function of mature cells. The brain exhibits one of the highest levels of tyrosine kinase activity in the adult animal and the synaptic region is particularly rich in tyrosine kinases and tyrosine phosphorylated proteins. Recent studies have described the effects of tyrosine phosphorylation on the activities of a number of proteins which are potentially involved in the regulation of synaptic function. Furthermore, it is becoming apparent that tyrosine phosphorylation is involved in the modification of synaptic activity, such as occurs during depolarization, the induction of long-term potentiation or long-term depression, and ischemia. Changes in the activities of tyrosine kinases and/or protein tyrosine phosphatases which are associated with synaptic structures may result in altered tyrosine phosphorylation of proteins located at the synapse leading to both short-term and long-lasting changes in synaptic and neuronal function.

journal_name

Neurochem Int

authors

Gurd JW

doi

10.1016/s0197-0186(97)00022-3

subject

Has Abstract

pub_date

1997-11-01 00:00:00

pages

635-49

issue

5

eissn

0197-0186

issn

1872-9754

pii

S0197-0186(97)00022-3

journal_volume

31

pub_type

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