Catch muscle myorod modulates ATPase activity of myosin in a phosphorylation-dependent way

Abstract

Myorod is expressed exclusively in molluscan catch muscle and localizes on the surface of thick filaments together with twitchin and myosin. Myorod is an alternatively spliced product of themyosin heavy-chain gene that contains the C-terminal rod part of myosin and a unique N-terminal domain. The unique domain is a target for phosphorylation by gizzard smooth myosin light chain kinase (smMLCK) and, perhaps, molluscan twitchin, which contains a MLCK-like domain. To elucidate the role ofmyorod and its phosphorylation in the catch muscle, the effect of chromatographically purifiedmyorod on the actin-activated Mg 2+ -ATPase activity of myosin was studied.We found that phosphorylation at the N-terminus of myorod potentiated the actin-activated Mg 2+ -ATPase activity ofmussel and rabbit myosins. This potentiation occurred only if myorod was phosphorylated and introduced into the ATPase assay as a co-filament with myosin. We suggest that myorod could be related to the catch state, a function specific to molluscan muscle.