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PINK1 is activated by mitochondrial membrane potential depolarization and stimulates Parkin E3 ligase activity by phosphorylating Serine 65.
Open Biol. 2012 May;2(5):120080. doi: 10.1098/rsob.120080.
Open Biol. 2012.
PMID: 22724072
Free PMC article.
Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65.
Kazlauskaite A, Kondapalli C, Gourlay R, Campbell DG, Ritorto MS, Hofmann K, Alessi DR, Knebel A, Trost M, Muqit MM.
Kazlauskaite A, et al. Among authors: kondapalli c.
Biochem J. 2014 May 15;460(1):127-39. doi: 10.1042/BJ20140334.
Biochem J. 2014.
PMID: 24660806
Free PMC article.
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Phosphoproteomic screening identifies Rab GTPases as novel downstream targets of PINK1.
Lai YC, Kondapalli C, Lehneck R, Procter JB, Dill BD, Woodroof HI, Gourlay R, Peggie M, Macartney TJ, Corti O, Corvol JC, Campbell DG, Itzen A, Trost M, Muqit MM.
Lai YC, et al. Among authors: kondapalli c.
EMBO J. 2015 Nov 12;34(22):2840-61. doi: 10.15252/embj.201591593. Epub 2015 Oct 15.
EMBO J. 2015.
PMID: 26471730
Free PMC article.
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The linker region in receptor guanylyl cyclases is a key regulatory module: mutational analysis of guanylyl cyclase C.
Saha S, Biswas KH, Kondapalli C, Isloor N, Visweswariah SS.
Saha S, et al. Among authors: kondapalli c.
J Biol Chem. 2009 Oct 2;284(40):27135-45. doi: 10.1074/jbc.M109.020032. Epub 2009 Jul 31.
J Biol Chem. 2009.
PMID: 19648115
Free PMC article.
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Aβ42 oligomers trigger synaptic loss through CAMKK2-AMPK-dependent effectors coordinating mitochondrial fission and mitophagy.
Lee A, Kondapalli C, Virga DM, Lewis TL Jr, Koo SY, Ashok A, Mairet-Coello G, Herzig S, Foretz M, Viollet B, Shaw R, Sproul A, Polleux F.
Lee A, et al. Among authors: kondapalli c.
Nat Commun. 2022 Aug 1;13(1):4444. doi: 10.1038/s41467-022-32130-5.
Nat Commun. 2022.
PMID: 35915085
Free PMC article.
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