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Mapping the Phosphorylation Sites of Ulk1

Dorsey, Frank C., Rose, Kristie L., Coenen, Silvia, Prater, Stephanie M., Cavett, Valerie, Cleveland, John L., Caldwell-Busby, Jennifer·2009·Journal of Proteome Research
DOI 10.1021/pr900583m
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Abstract

Ulk1 is a serine/threonine kinase that controls macroautophagy, an essential homeostatic recycling pathway that degrades bulk cytoplasmic material and directs the turnover of organelles such as peroxisomes and mitochondria. Further, macroautophagy is potently induced by signals that trigger metabolic stress, such as hypoxia and amino acid starvation, where its recycling functions provide macromolecules necessary to maintain catabolic metabolism and cell survival. Substrates for Ulk1 have not been identified, and little is known regarding post-translational control of Ulk1 kinase activity and function. To gain insights into the regulatory mechanisms of Ulk1, we developed a robust purification protocol for Ulk1 and demonstrated that Ulk1 is highly phosphorylated and requires autophosphorylation for stability. Importantly, high-resolution, tandem mass spectrometry identified multiple sites of phosphorylation on Ulk1, including several within domains known to regulate macroautophagy. Differential phosphorylation analyses also identified sites of phosphorylation in the C-terminal domain that depend upon or require Ulk1 autophosphorylation.

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Metadata

Authors
Dorsey, F. C., Rose, K. L., Coenen, S., Prater, S. M., Cavett, V., Cleveland, J. L., & Caldwell-Busby, J.
Affiliations
Departments of Cancer Biology and Molecular Therapeutics and The Translational Research Institute, The Scripps Research Institute, Jupiter, Florida 33458, and Max Planck Institute of Biochemistry, Martinsried, Germany
Venue
Journal of Proteome Research
Publisher
American Chemical Society (ACS)
Published
2009-10-19
Volume
8
Issue
11
Pages
5253-5263
ISSN
  • 1535-3893
  • 1535-3907
DOI
10.1021/pr900583m
Cited by
72
References
4
Language
en

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