SUMOylation does not affect cardiac troponin I stability but alters indirectly the development of force in response to Ca(2+)

Post‐translational modification of the myofilament protein troponin I by phosphorylation is known to trigger functional changes that support enhanced contraction and relaxation of the heart. We report for the first time that human troponin I can also be modified by SUMOylation at lysine 177. Functio...

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Detalles Bibliográficos
Autores principales: Fertig, Bracy, Ling, Jiayue, Nollet, Edgar E., Dobi, Sara, Busiau, Tara, Ishikawa, Kiyotake, Yamada, Kelly, Lee, Ahyoung, Kho, Changwon, Wills, Lauren, Tibbo, Amy J., Scott, Mark, Grant, Kirsten, Campbell, Kenneth S., Birks, Emma J., MacQuaide, Niall, Hajjar, Roger, Smith, Godfrey L., van der Velden, Jolanda, Baillie, George S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2022
Materias:
Original Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9588612/
https://www.ncbi.nlm.nih.gov/pubmed/35633070
http://dx.doi.org/10.1111/febs.16537
Descripción
Sumario:Post‐translational modification of the myofilament protein troponin I by phosphorylation is known to trigger functional changes that support enhanced contraction and relaxation of the heart. We report for the first time that human troponin I can also be modified by SUMOylation at lysine 177. Functionally, TnI SUMOylation is not a factor in the development of passive and maximal force generation in response to calcium, however this modification seems to act indirectly by preventing SUMOylation of other myofilament proteins to alter calcium sensitivity and cooperativity of myofilaments. Utilising a novel, custom SUMO site‐specific antibody that recognises only the SUMOylated form of troponin I, we verify that this modification occurs in human heart and that it is upregulated during disease.

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