Journal article

The secret life of kinases: insights into non-catalytic signalling functions from pseudokinases

Annette V Jacobsen, James M Murphy

BIOCHEMICAL SOCIETY TRANSACTIONS | PORTLAND PRESS LTD | Published : 2017

Abstract

Over the past decade, our understanding of the mechanisms by which pseudokinases, which comprise ∼10% of the human and mouse kinomes, mediate signal transduction has advanced rapidly with increasing structural, biochemical, cellular and genetic studies. Pseudokinases are the catalytically defective counterparts of conventional, active protein kinases and have been attributed functions as protein interaction domains acting variously as allosteric modulators of conventional protein kinases and other enzymes, as regulators of protein trafficking or localisation, as hubs to nucleate assembly of signalling complexes, and as transmembrane effectors of such functions. Here, by categorising mammalia..

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University of Melbourne Researchers

Grants

Awarded by National Health and Medical Research Council of Australia (NHMRC) fellowship


Awarded by NHMRC Project grants


Awarded by NHMRC IRIISS


Funding Acknowledgements

A.V.J. is supported by an Australian Government Research Training Program Scholarship and J.M.M. is supported by the National Health and Medical Research Council of Australia (NHMRC) fellowship [1105754]. Our work reviewed herein was supported by NHMRC Project grants [ 1057905, 1067289, 1124735, and 1124737], NHMRC IRIISS 9000220, and Victorian Government Operational Infrastructure Support.