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Acetylation stabilises calmodulin-regulated calcium signalling

Baker, Karen, Geeves, Michael A., Mulvihill, Daniel P. (2022) Acetylation stabilises calmodulin-regulated calcium signalling. FEBS Letters, . pp. 762-771. ISSN 1873-3468. E-ISSN 1873-3468. (doi:10.1002/1873-3468.14304) (KAR id:92803)

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Calmodulin is a conserved calcium signalling protein that regulates a wide range of cellular functions. Amino-terminal acetylation is a ubiquitous posttranslational modification that affects ~ 90% of all human proteins, to stabilise structure, as well as regulate function and proteolytic degradation. Here we present data on the impact of amino-terminal acetylation upon structure and calcium signalling function of fission yeast calmodulin. We show NatA dependent acetylation stabilises the helical structure of the S. pombe calmodulin, impacting its ability to associate with myosin at endocytic foci. We go on to show this conserved modification impacts both the calcium binding capacity of yeast and human calmodulins. These findings have significant implications for research undertaken into this highly conserved essential protein.

Item Type: Article
DOI/Identification number: 10.1002/1873-3468.14304
Projects: Development of a rapid temperature jump system for live in vivo microscopy., ynthetic bacterial vesicles to enhance recombinant protein production, delivery and isolation for Industrial Biotechnology applications.
Uncontrolled keywords: Schizosaccharomyces pombe, acetylation, myosin, endocytosis, calmodulin
Subjects: Q Science > QH Natural history > QH301 Biology
Q Science > QH Natural history > QH581.2 Cell Biology
Q Science > QP Physiology (Living systems) > QP506 Molecular biology
Q Science > QP Physiology (Living systems) > QP517 Biochemistry
Divisions: Divisions > Division of Natural Sciences > Industrial Biotechnology Centre
Divisions > Division of Natural Sciences > Biosciences
Funders: Biotechnology and Biological Sciences Research Council (
Depositing User: Daniel Mulvihill
Date Deposited: 21 Jan 2022 13:40 UTC
Last Modified: 04 Sep 2023 09:34 UTC
Resource URI: (The current URI for this page, for reference purposes)
Baker, Karen:
Geeves, Michael A.:
Mulvihill, Daniel P.:
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