[A new actin-binding area of the myosin light chains' high-molecular kinase].
High-molecular weight isoform of myosin light chain kinase (MLCK-210) contains a unique N-terminal domain not present in a low-molecular weight isoform, MLCK-108. Functional features of this domain are poorly studied. We provide evidence that N-terminal area of the unique MLCK-210 domain incorporates previously unrecognized actin-binding region that could be involved in the interaction of MLCK-210 with the actin cytoskeleton.
Vilitkevich
E L
EL
Kudriashev
D S
DS
Stepanova
O V
OV
Shirinskiĭ
V P
VP
D000199:Actins / Q000737:chemistry* / Q000378:metabolism; D000818:Animals; D002460:Cell Line; D002522:Chlorocebus aethiops; D003599:Cytoskeleton / Q000378:metabolism; D007527:Isoenzymes / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D018482:Muscle, Skeletal / Q000737:chemistry*; D009219:Myosin-Light-Chain Kinase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011485:Protein Binding / Q000235:genetics; D017434:Protein Structure, Tertiary / Q000235:genetics; D011817:Rabbits; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
D000199:Actins; D007527:Isoenzymes; D011994:Recombinant Proteins; D009219:Myosin-Light-Chain Kinase