caa a22 4500 606177272 CHVBK 20210128100751.0 cr unu---uuuuu 210128e20151101xx s 000 0 eng 10.1007/s00018-015-1996-x doi (NATIONALLICENCE)springer-10.1007/s00018-015-1996-x Regulation of αA- and αB-crystallins via phosphorylation in cellular homeostasis [Elektronische Daten] [Erin Thornell, Andrew Aquilina] αA-Crystallin (αA) and αB-crystallin (αB) are small heat shock proteins responsible for the maintenance of transparency in the lens. In non-lenticular tissues, αB is involved in both maintenance of the cytoskeleton and suppression of neurodegeneration amongst other roles. Despite their importance in maintaining cellular health, modifications and mutations to αA and αB appear to play a role in disease states such as cataract and myopathies. The list of modifications that have been reported is extensive and include oxidation, disulphide bond formation, C- and N-terminal truncation, acetylation, carboxymethylation, carboxyethylation, carbamylation, deamidation, phosphorylation and methylation. Such modifications, notably phosphorylation, are alleged to cause changes to chaperone activity by inducing substructural changes and altering subunit exchange dynamics. Although the effect modification has on the activities of αA and αB is contentious, it has been proposed that these changes are responsible for the induction of hyperactivity and are thereby indirectly responsible for protein deposition characteristic of many diseases associated with αA and αB. This review compiles all reported sites of αA and αB modifications, and investigates the role phosphorylation, in particular, plays in cellular processes. Springer Basel, 2015 Chaperones nationallicence PTMs nationallicence Structure nationallicence Proteostasis nationallicence Thornell Erin Illawarra Health and Medical Research Institute, University of Wollongong, Northfields Ave., 2522, Wollongong, NSW, Australia aut Aquilina Andrew Illawarra Health and Medical Research Institute, University of Wollongong, Northfields Ave., 2522, Wollongong, NSW, Australia aut Cellular and Molecular Life Sciences Springer Basel 72/21(2015-11-01), 4127-4137 1420-682X 72:21<4127 2015 72 18 https://doi.org/10.1007/s00018-015-1996-x text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 review-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00018-015-1996-x text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Thornell Erin Illawarra Health and Medical Research Institute, University of Wollongong, Northfields Ave., 2522, Wollongong, NSW, Australia aut NATIONALLICENCE 700 1- Aquilina Andrew Illawarra Health and Medical Research Institute, University of Wollongong, Northfields Ave., 2522, Wollongong, NSW, Australia aut NATIONALLICENCE 773 0- Cellular and Molecular Life Sciences Springer Basel 72/21(2015-11-01), 4127-4137 1420-682X 72:21<4127 2015 72 18