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- Title
PINK1 activation - turning on a promiscuous kinase.
- Authors
Aerts, Liesbeth; De Strooper, Bart; Morais, Vanessa A.
- Abstract
PINK1 [phosphatase and tensin homologue (PTEN)-induced putative kinase 1] is a serine/threonine kinase targeted to mitochondria and implicated in early-onset recessive Parkinson's disease (PD). Through the phosphorylation of its downstream targets, PINK1 regulates multiple mitochondrial processes, including ATP production, stress-response and mitochondrial dynamics and quality control. The orchestration of such a wide array of functions by an individual kinase requires a fine-tuned and versatile regulation of its activity. PINK1 proteolytic processing, trafficking and localization, as well as different post-translational modifications, affect its activity and function. Unravelling the regulatory mechanisms of PINK1 is essential for a full comprehension of its kinase function in health and disease.
- Subjects
SERINE/THREONINE kinases; MITOCHONDRIA; PARKINSON'S disease; PHOSPHORYLATION; POST-translational modification
- Publication
Biochemical Society Transactions, 2015, Vol 43, Issue 2, p280
- ISSN
0300-5127
- Publication type
Article
- DOI
10.1042/BST20150002