Research Papers:

Identification of novel Ack1-interacting proteins and Ack1 phosphorylated sites in mouse brain by mass spectrometry

Maria del Mar Masdeu, Beatriz G. Armendáriz, Anna La Torre, Eduardo Soriano _, Ferran Burgaya and Jesús Mariano Ureña

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Oncotarget. 2017; 8:101146-101157. https://doi.org/10.18632/oncotarget.20929

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Maria del Mar Masdeu1,2,3,#, Beatriz G. Armendáriz1,2,#, Anna La Torre1,4, Eduardo Soriano1,2,5,6, Ferran Burgaya1,2,* and Jesús Mariano Ureña1,2,*

1Department of Cell Biology, Faculty of Biology, University of Barcelona, Barcelona 08028, Spain

2Centro de Investigación Biomédica en Red sobre Enfermedades Neurodegenerativas (CIBERNED), ISCIII, 28031 Madrid, Spain

3Present address: Francis Crick Institute, Mill Hill Laboratory, Mill Hill, London NW7 1AA, United Kingdom

4Present address: Department of Cell Biology and Human Anatomy, University of California Davis, 95616 Davis, California, USA

5Vall d´Hebron Institute of Research, Barcelona 08035, Spain

6Institució Catalana de Recerca i Estudis Avançats (ICREA), Barcelona 08010, Spain

*Co-senior authors

#These authors contributed equally to this work

Correspondence to:

Eduardo Soriano, email: [email protected]

Ferran Burgaya, email: [email protected]

Jesús Mariano Ureña, email: [email protected]

Keywords: tyrosine kinase, Ack1, central nervous system, development

Received: April 21, 2017     Accepted: August 26, 2017     Published: September 15, 2017


Ack1 (activated Cdc42-associated tyrosine kinase) is a non-receptor tyrosine kinase that is highly expressed in brain. This kinase contains several protein-protein interaction domains and its action is partially regulated by phosphorylation. As a first step to address the neuronal functions of Ack1, here we screened mouse brain samples to identify proteins that interact with this kinase. Using mass spectrometry analysis, we identified new putative partners for Ack1 including cytoskeletal proteins such as Drebrin or MAP4; adhesion regulators such as NCAM1 and neurabin-2; and synapse mediators such as SynGAP, GRIN1 and GRIN3. In addition, we confirmed that Ack1 and CAMKII both co-immunoprecipitate and co-localize in neurons. We also identified that adult and P5 samples contained the phosphorylated residues Thr 104 and Ser 825, and only P5 samples contained phosphorylated Ser 722, a site linked to cancer and interleukin signaling when phosphorylated. All these findings support the notion that Ack1 could be involved in neuronal plasticity.

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