{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,14]],"date-time":"2026-10-14T18:20:46Z","timestamp":1792002046317,"version":"4.4.0"},"reference-count":144,"publisher":"MDPI AG","issue":"12","license":[{"start":{"date-parts":[[2024,12,22]],"date-time":"2024-12-22T00:00:00Z","timestamp":1734825600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biomolecules"],"abstract":"<jats:p>The maintenance of healthy mitochondria is essential for neuronal survival and relies upon mitochondrial quality control pathways involved in mitochondrial biogenesis, mitochondrial dynamics, and mitochondrial autophagy (mitophagy). Mitochondrial dysfunction is critically implicated in Parkinson\u2019s disease (PD), a brain disorder characterized by the progressive loss of dopaminergic neurons in the substantia nigra. Consequently, impaired mitochondrial quality control may play a key role in PD pathology. This is affirmed by work indicating that genes such as PRKN and PINK1, which participate in multiple mitochondrial processes, harbor PD-associated mutations. Furthermore, mitochondrial complex-I-inhibiting toxins like MPTP and rotenone are known to cause Parkinson-like symptoms. At the heart of PD is alpha-synuclein (\u03b1S), a small synaptic protein that misfolds and aggregates to form the disease\u2019s hallmark Lewy bodies. The specific mechanisms through which aggregated \u03b1S exerts its neurotoxicity are still unknown; however, given the vital role of both \u03b1S and mitochondria to PD, an understanding of how \u03b1S influences mitochondrial maintenance may be essential to elucidating PD pathogenesis and discovering future therapeutic targets. Here, the current knowledge of the relationship between \u03b1S and mitochondrial quality control pathways in PD is reviewed, highlighting recent findings regarding \u03b1S effects on mitochondrial biogenesis, dynamics, and autophagy.<\/jats:p>","DOI":"10.3390\/biom14121649","type":"journal-article","created":{"date-parts":[[2024,12,23]],"date-time":"2024-12-23T04:33:29Z","timestamp":1734928409000},"page":"1649","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":28,"title":["Alpha-Synuclein Effects on Mitochondrial Quality Control in Parkinson\u2019s Disease"],"prefix":"10.3390","volume":"14","author":[{"given":"Lydia","family":"Shen","sequence":"first","affiliation":[{"name":"College of Arts & Sciences, Cornell University, Ithaca, NY 14853, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6676-0107","authenticated-orcid":false,"given":"Ulf","family":"Dettmer","sequence":"additional","affiliation":[{"name":"Ann Romney Center for Neurologic Diseases, Brigham and Women\u2019s Hospital and Harvard Medical School, Boston, MA 02115, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2024,12,22]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"939","DOI":"10.1016\/S1474-4422(18)30295-3","article-title":"Global, Regional, and National Burden of Parkinson\u2019s Disease, 1990\u20132016: A Systematic Analysis for the Global Burden of Disease Study 2016","volume":"17","author":"Dorsey","year":"2018","journal-title":"Lancet Neurol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"896","DOI":"10.1016\/S0140-6736(14)61393-3","article-title":"Parkinson\u2019s disease","volume":"386","author":"Kalia","year":"2015","journal-title":"Lancet"},{"key":"ref_3","unstructured":"Stoker, T.B., and Greenland, J.C. 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