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Identification of AMPK Phosphorylation Sites Reveals a Network of Proteins Involved in Cell Invasion and Facilitates Large-Scale Substrate Prediction

Schaffer, Bethany E., Levin, Rebecca S., Hertz, Nicholas T., Maures, Travis J., Schoof, Michael L., Hollstein, Pablo E., Benayoun, Bérénice A., Banko, Max R., Shaw, Reuben J., Shokat, Kevan M., Brunet, Anne·2015·Cell Metabolism
DOI 10.1016/j.cmet.2015.09.009PMC PMC4635044
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  • Several residues in SNX17 CT near the NxxY/F motif could be phosphorylated, including S434, S437, and S440, which may modulate the autoinhibition mechanism.

    “In addition, several residues in SNX17 CT near the NxxY/F motif could be phosphorylated, including S434, S43742, and S440, which may modulate the autoinhibition mechanism.”

    From Structural basis for Retriever-SNX17 assembly and endosomal sorting (2024) · cites this paper as [42]

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Research works printed but not linked: 53

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Metadata

Authors
Schaffer, B. E., Levin, R. S., Hertz, N. T., Maures, T. J., Schoof, M. L., Hollstein, P. E., Benayoun, B. A., Banko, M. R., Shaw, R. J., Shokat, K. M., & Brunet, A.
Venue
Cell Metabolism
Publisher
Elsevier BV
Published
2015-11
Volume
22
Issue
5
Pages
907-921
ISSN
1550-4131
DOI
10.1016/j.cmet.2015.09.009
PMC
PMC4635044
Cited by
184
References
8
Language
en
Licence

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