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a novel, heterozygous p.Glu11Lys mutation in the atrial-specific myosin light chain gene MYL4, caused atrial fibrillation.
A recessive frameshift mutation in MYL4 causes early-onset atrial fibrillation.
The (Ala-Pro) rich part of this protein acts as a "spacer arm" responsible for correct positioning of the N-terminal actin binding site.
The N-terminus of this protein is an actin binding site.
NMR showed involvement of N-terminus and lysines 3 and 4 in interaction with actin. Mutations of these lysines (K3A,K4R,K4A,K4D) resulted in altered actin binding and actin activated MgATPase. Mutation of Ala-1 to val had no effect on binding or kinetics.
Gene expression of myosin light chain 1 atrial isoform is regulated by BOB.1/OBF (show IZUMO1 Proteins).1 coactivator.
Myosin is a hexameric ATPase cellular motor protein. It is composed of two myosin heavy chains, two nonphosphorylatable myosin alkali light chains, and two phosphorylatable myosin regulatory light chains. This gene encodes a myosin alkali light chain that is found in embryonic muscle and adult atria. Two alternatively spliced transcript variants encoding the same protein have been found for this gene.
myosin light chain 1, atrial isoform
, myosin light chain 4
, myosin light chain 1, embryonic muscle/atrial isoform
, myosin light chain alkali GT-1 isoform
, myosin, atrial/fetal muscle, light chain
, myosin, light polypeptide 4, alkali; atrial, embryonic
, myosin light chain 1, atrial/fetal isoform
, myosin light chain, alkali, cardiac atria