Journal
BIOCHEMICAL SOCIETY TRANSACTIONS
Volume 34, Issue -, Pages 842-845Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BST0340842
Keywords
binding partner; extracellular-signal-regulated kinase (ERK); mitogen-activated protein kinase (MAPK); nuclear export; phosphorylation; protein phosphatase
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ERK (extracellular-signal-regulated kinase) is a MAPK (mitogen-activated protein kinase), which regulates diverse physiological functions including cell proliferation, differentiation, transformation and survival. it is now clear that in addition to the duration and magnitude of signalling through this MAPK pathway, the spatial restriction of MAPK activity plays a key role in determining the physiological outcome of signalling. Recent work has led to the discovery of MAPK-binding proteins, which contain either nuclear localization signals or nuclear export signals. These include MAPK activators and specific protein phosphatases, which may act to both regulate MAPK activity and the subcellular localization of their substrate. This represents a mechanism by which signalling in response to extracellular stimuli may be modulated in terms of both magnitude/duration and spatial restriction thus allowing differential access of the activated MAPK to target proteins and the interpretation of this information by cells to determine an appropriate physiological response.
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