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Are biological sensors modulated by their structural scaffolds? The role of the structural muscle proteins α‐actinin‐2 and α‐actinin‐3 as modulators of biological sensors
Author(s) -
Lek Monkol,
North Kathryn N.
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.05.059
Subject(s) - actinin , skeletal muscle , microbiology and biotechnology , chemistry , function (biology) , protein–protein interaction , phenotype , biophysics , biology , biochemistry , cytoskeleton , anatomy , cell , gene
Biological sensors and their ability to detect and respond to change in the cellular environment can be modulated by protein scaffolds acting within their interaction network. The skeletal muscle α‐actinins have been considered as primarily structural scaffold proteins. However, deficiency of α‐actinin‐3 due to a common null polymorphism results in predominantly metabolic changes in skeletal muscle function. In this review, we explore the range of phenotypes associated with α‐actinin‐3 deficiency, and draw supporting evidence from known interaction partners for its role as a scaffold which acts to modulate biological sensors that result in changes in muscle metabolism and structure.