Abstract
The myosin family is a large inventory of actin-associated motor proteins that participate in a diverse array of cellular functions. Several myosin classes are expressed in neural cells and play important roles in neural functioning. A recently discovered member of the myosin superfamily, the vertebrate-specific myosin XVI (Myo16) class is expressed predominantly in neural tissues and appears to be involved in the development and proper functioning of the nervous system. Accordingly, the alterations of MYO16 has been linked to neurological disorders. Although the role of Myo16 as a generic actin-associated motor is still enigmatic, the N-, and C-terminal extensions that flank the motor domain seem to confer unique structural features and versatile interactions to the protein. Recent biochemical and physiological examinations portray Myo16 as a signal transduction element that integrates cell signaling pathways to actin cytoskeleton reorganization. This review discusses the current knowledge of the structure-function relation of Myo16. In light of its prevalent localization, the emphasis is laid on the neural aspects.
Highlights
Myosins are actin-based mechanochemical machines that convert the chemical energy of ATP hydrolysis to mechanical work and molecular movement along actin filaments [1,2]
The confined expression in neural tissues, the structural characteristics and interactions of the vertebrate-specific unconventional myosin XVI class suggest that it has an important role in neural development and functioning
As a support of this, the genetic examinations underscore the significance of Myo16 in the pathomechanism of neurological disorders, such as schizophrenia, autism spectrum disorder, bipolar disorder subtype II and major depressive disorder
Summary
Myosins are actin-based mechanochemical machines that convert the chemical energy of ATP hydrolysis to mechanical work and molecular movement along actin filaments [1,2]. The predominant expression of Myo in neural tissues suggests its importance in the proper functioning of the brain, mainly during development and in adulthood. Based on the recent biochemical and physiological analyses, Myo is emerging as an important regulator of the proper functioning of neural cells, the exact molecular mechanisms underlying its role in the nervous system remain to be elucidated. We provide an overview of the current understanding of the structural features, molecular interactions and cellular roles of Myo in the nervous system focusing on its unique domains: the N-terminal Myo16Ank and the C-terminal. N-terminal composed of an N-terminal ankyrin domain (Myo16Ank) possessing a conserved myosin element (MyPhoNE), a KVxF sequence motif (protein phosphatase type 1 catalytic subunit type (PP1c) phosphatase. Myo16Ank is followed by the motor domain, a single catalytic subunit (PP1c) binding motif) and eight ankyrin repeats (Ank). The phosphotyrosines (Y1416 and Y1441) in the NHM motif are indicated (pY)
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