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Article

Focal segmental glomerulosclerosis ACTN4 mutants binding to actin: regulation by phosphomimetic mutations.

Scientific reports - 29 Oct 2019

Shao Hanshuang, Wingert Bentley, Weins Astrid, Pollak Martin R, Camacho Carlos, Wells Alan

Abstract excerpt

Natural mutations such as lysine 255 to glutamic acid (K to E), threonine 259 to isoleucine (T to I) and serine 262 to proline (S to P) that occur within the actin binding domain of alpha-actinin-4 (ACTN4) cause an autosomal dominant form of focal segmental glomerulosclerosis (FSGS) in affected humans. This appears due to elevated actin binding propensity in podocytes resulting in a 'frozen' cytoskeleton. What is...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 31664084
DOI: 10.1038/s41598-019-51825-2
PMCID: PMC6820738

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