MPI-INF D3 Publications: Journal Article: Specificity of linear motifs that bind to a common mitogen-activated protein kinase docking groove

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Author, Editor(s)

Author(s):

Garai, Ágnes
Zeke, András
Gógl, Gergo
Töro, Imre
Fördos, Ferenc
Blankenburg, Hagen
Bárkai, Tünde
Varga, János
Alexa, Anita
Emig, Dorothea
Albrecht, Mario
Reményi, Attila

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Not MPG Author(s):

Garai, Ágnes
Zeke, András
Gógl, Gergo
Töro, Imre
Fördos, Ferenc
Bárkai, Tünde
Varga, János
Alexa, Anita
Reményi, Attila

BibTeX cite key*:

Albrecht2012e

Title

Title*:

Specificity of linear motifs that bind to a common mitogen-activated protein kinase docking groove

Journal

Journal Title*:	Science Signaling	Journal's URL:	http://stke.sciencemag.org/
Download URL for the article:	http://stke.sciencemag.org/cgi/reprint/sigtrans;5/245/ra74.pdf	Language:	English

Publisher

Publisher's Name:	AAAS	Publisher's URL:
Publisher's Address:	Washington, DC	ISSN:	1937-9145

Vol, No, pp, Date

Volume*:	5	Number:	245
Publishing Date:	2012
Pages*:	ra74,1-ra74,14	Number of VG Pages:
Page Start:	ra74,1	Page End:	ra74,14
Sequence Number:	ra74	DOI:	10.1126/scisignal.2003004

Note:
(LaTeX) Abstract:	Mitogen-activated protein kinases (MAPKs) have a docking groove that interacts with linear "docking" motifs in binding partners. To determine the structural basis of binding specificity between MAPKs and docking motifs, we quantitatively analyzed the ability of 15 docking motifs from diverse MAPK partners to bind to c-Jun amino-terminal kinase 1 (JNK1), p38α, and extracellular signal–regulated kinase 2 (ERK2). Classical docking motifs mediated highly specific binding only to JNK1, and only those motifs with a sequence pattern distinct from the classical MAPK binding docking motif consensus differentiated between the topographically similar docking grooves of ERK and p38α. Crystal structures of four complexes of MAPKs with docking peptides, representing JNK-specific, ERK-specific, or ERK- and p38-selective binding modes, revealed that the regions located between consensus positions in the docking motifs showed conformational diversity. Although the consensus positions in the docking motifs served as anchor points that bound to common MAPK surface features and mostly contributed to docking in a nondiscriminatory fashion, the conformation of the intervening region between the anchor points mostly determined specificity. We designed peptides with tailored MAPK binding profiles by rationally changing the length and amino acid composition of intervening regions located between anchor points. These results suggest a coherent structural model for MAPK docking specificity that reveals how short linear motifs binding to a common kinase docking groove can mediate diverse interaction patterns and contribute to correct MAPK partner selection in signaling networks.
URL for the Abstract:	http://dx.doi.org/doi:10.1126/scisignal.2003004
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Download Access Level:	Internal

Correlation

MPG Unit:	Max-Planck-Institut für Informatik

MPG Subunit:	Computational Biology and Applied Algorithmics
Appearance:	MPII WWW Server, MPII FTP Server, MPG publications list, university publications list, working group publication list, Fachbeirat, VG Wort

BibTeX Entry:

@ARTICLE{Albrecht2012e,
AUTHOR = {Garai, Ágnes and Zeke, Andr{\'a}s and G{\"o}gl, Gergo and T{\"o}ro, Imre and F{\"o}rdos, Ferenc and Blankenburg, Hagen and B{\'a}rkai, T{\"u}nde and Varga, J{\'a}nos and Alexa, Anita and Emig, Dorothea and Albrecht, Mario and Rem{\'e}nyi, Attila},
TITLE = {Specificity of linear motifs that bind to a common mitogen-activated protein kinase docking groove},
JOURNAL = {Science Signaling},
PUBLISHER = {AAAS},
YEAR = {2012},
NUMBER = {245},
VOLUME = {5},
PAGES = {ra74,1--ra74,14},
ADDRESS = {Washington, DC},
ISBN = {1937-9145},
DOI = {10.1126/scisignal.2003004},
}

Entry last modified by Anja Becker, 02/12/2013

Edit History (please click the blue arrow to see the details)

	Editor(s) [Library]	Created 12/19/2012 11:43:50
Revisions 2. 1. 0.	Editor(s) Anja Becker Mario Albrecht Nadezhda Tsankova Doncheva	Edit Dates 12.02.2013 16:07:35 01/05/2013 01:14:47 AM 12/19/2012 11:43:50 AM