MYH13, a superfast myosin expressed in extraocular, laryngeal, and syringeal muscles

Stefano Schiaffino, Simon Hughes, Marta Murgia, Carlo Reggiani

Research output: Contribution to journalReview articlepeer-review

Abstract

MYH13 is a unique type of sarcomeric myosin heavy chain (MYH) first detected in mammalian extraocular (EO) muscles and later also in vocal muscles, including laryngeal muscles of some mammals and syringeal muscles of songbirds. All these muscles are specialized in generating very fast contractions while producing relatively low force, a design appropriate for muscles acting against a much lower load than most skeletal muscles inserting into the skeleton. The definition of the physiological properties of muscle fibers containing MYH13 has been complicated by the mixed fiber type composition of EO muscles and the coexistence of different MYH types within the same fiber. A major advance in this area came from studies on isolated recombinant myosin motors and the demonstration that the affinity of actin-bound human MYH13 for ADP is much weaker than those of fast-type MYH1 (type 2X) and MYH2 (type 2A). This property is consistent with a very fast detachment of myosin from actin, a major determinant of shortening velocity. The MYH13 gene arose early during vertebrate evolution but has been characterized only in mammals and birds and appears to have been lost in some teleost fish. The MYH13 gene is located at the 3’ end of the mammalian fast/developmental gene cluster and in a similar position of the orthologous cluster in syntenic regions of the songbird genome. MYH13 gene regulation is controlled by a super-enhancer in the mammalian locus and deletion of the neighboring fast MYH1 and MYH4 genes leads to abnormal MYH13 expression in mouse leg muscles.
Original languageEnglish
JournalJ Physiol - London
Publication statusAccepted/In press - 30 Nov 2023

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