Spatio-temporal regulation of mitogen-activated protein kinase (MAPK) signalling by protein phosphatases

M. Karlsson, M. Mandl, S M Keyse

    Research output: Contribution to journalArticlepeer-review

    25 Citations (Scopus)

    Abstract

    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.
    Original languageEnglish
    Pages (from-to)842-5
    Number of pages4
    JournalBiochemical Society Transactions
    Volume34
    Issue number5
    DOIs
    Publication statusPublished - 2006

    Keywords

    • binding partner
    • ERK
    • MAPK
    • Nuclear export
    • Phosphorylation
    • protein phosphatase

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