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Molecular and Cellular Biology, February 2001, p. 1218-1227, Vol. 21, No. 4
Centro de Biología Molecular
"Severo Ochoa," Consejo Superior de Investigaciones
Científicas-Universidad Autónoma de Madrid,
Universidad Autónoma, 28049 Madrid, Spain
Received 8 September 2000/Returned for modification 22 October
2000/Accepted 21 November 2000
The MEK5-extracellular signal-regulated kinase (ERK5) tandem is a
novel mitogen-activated protein kinase cassette critically involved in
mitogenic activation by the epidermal growth factor (EGF). The atypical
protein kinase C isoforms (aPKCs) have been shown to be required for
cell growth and proliferation and have been reported to interact with
the adapter protein p62 through a short stretch of acidic amino acids
termed the aPKC interaction domain. This region is also present in
MEK5, suggesting that it may be an aPKC-binding partner. Here we
demonstrate that the aPKCs interact in an EGF-inducible manner with
MEK5 and that this interaction is required and sufficient for the
activation of MEK5 in response to EGF. Consistent with the role of the
aPKCs in the MEK5-ERK5 pathway, we show that
0270-7306/01/$04.00+0 DOI: 10.1128/MCB.21.4.1218-1227.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
MEK5, a New Target of the Atypical Protein Kinase
C Isoforms in Mitogenic Signaling
PKC and
/
PKC
activate the Jun promoter through the MEF2C element, a well-established
target of ERK5. From all these results, we conclude that MEK5 is a
critical target of the aPKCs during mitogenic signaling.
*
Corresponding author. Mailing address: Centro de
Biología Molecular "Severo Ochoa," (CSIC), Universidad
Autónoma, Canto Blanco, 28049 Madrid, Spain. Phone:
34-913978039. Fax: 34-629690055. E-mail:
jmoscat{at}cbm.uam.es.
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