PINK1 in the limelight: multiple functions of an eclectic protein in human health and disease
The gene PINK1 [phosphatase and tensin homologue (PTEN)‐induced putative kinase 1] encodes a serine/threonine kinase which was initially linked to the pathogenesis of a familial form of Parkinson's disease. Research on PINK1 has recently unravelled that its multiple functions extend well beyond...
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Published in: | The Journal of pathology Vol. 241; no. 2; pp. 251 - 263 |
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Main Authors: | , |
Format: | Journal Article |
Language: | English |
Published: |
Chichester, UK
John Wiley & Sons, Ltd
01-01-2017
Wiley Subscription Services, Inc |
Subjects: | |
Online Access: | Get full text |
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Summary: | The gene PINK1 [phosphatase and tensin homologue (PTEN)‐induced putative kinase 1] encodes a serine/threonine kinase which was initially linked to the pathogenesis of a familial form of Parkinson's disease. Research on PINK1 has recently unravelled that its multiple functions extend well beyond neuroprotection, implicating this eclectic protein in a growing number of human pathologies, including cancer, diabetes, cardiopulmonary dysfunctions, and inflammation. Extensive studies have identified PINK1 as a crucial player in the mitochondrial quality control pathway, required to label damaged mitochondria and promote their elimination through an autophagic process (mitophagy). Mounting evidence now indicates that PINK1 activities are not restricted solely to mitophagy, and that different subcellular and even sub‐mitochondrial pools of PINK1 are involved in distinct signalling cascades to regulate cell metabolism and survival. In this review, we provide a concise overview on the different functions of PINK1 and their potential role in human diseases. Copyright © 2016 Pathological Society of Great Britain and Ireland. Published by John Wiley & Sons, Ltd. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-3 content type line 23 ObjectType-Review-1 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 0022-3417 1096-9896 |
DOI: | 10.1002/path.4815 |