PINK1 activation–turning on a promiscuous kinase. (7th April 2015)

• Record Type: Journal Article
• Authors: Aerts, Liesbeth; De Strooper, Bart; Morais, Vanessa A.
• Is Part Of: Biochemical Society transactions. Volume 43:Number 2(2015)
• Page Start: 280
• Page End: 286
• Publication Date: 2015-04-07
• Subjects: mitochondria -- phosphatase and tensin homologue-induced putative kinase 1 (PINK1) -- Parkinson's disease -- phosphorylation -- serine/threonine kinase; Biochemistry -- Congresses; 572
• DOI: 10.1042/BST20150002
• Languages: English
• ISSNs: 0300-5127

Abstract

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.