Myosins

Heissler, S.M.; Sellers, J.R.

doi:10.1016/b978-0-12-394447-4.20059-x

Cited by 8 publications

(10 citation statements)

References 109 publications

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“…It is of note that not each of the regulatory mechanisms listed is applicable to each member in a given myosin class. The reader is redirected to comprehensive reviews for the detailed physiological function of individual members of a given myosin class [3, 4]. Motors indicate the number of myosin motor domains in the minimum functional unit of the protein.…”

Section: Figmentioning

confidence: 99%

“…Family members are widely expressed and tightly integrated in cellular networks of interlinked biochemical pathways where they function as integrators between signaling and the dynamics of cytoskeletal mechanics [1–4]. As highly allosteric enzymes, the stringent regulation is a prerequisite for myosin’s function in active transport processes, cytoplasmic contractility, and mechanosensing in both physiological and pathological processes [2–5].…”

Section: Introductionmentioning

confidence: 99%

“…As individual members of a myosin class are sometimes synergistically targeted by different regulatory mechanisms, a single myosin class may be discussed in multiple sections of this review. The detailed discussion of individual myosin classes is beyond the current work and can be found in exhaustive recent reviews [3, 4]. …”

Section: Introductionmentioning

confidence: 99%

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Various Themes of Myosin Regulation

Heissler

Sellers

2016

Journal of Molecular Biology

117

127

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Members of the myosin superfamily are actin-based molecular motors that are indispensable for cellular homeostasis. The vast functional and structural diversity of myosins accounts for the variety and complexity of the underlying allosteric regulatory mechanisms that determine the activation or inhibition of myosin motor activity and enable precise timing and spatial aspects of myosin function at the cellular level. This review focuses on the molecular basis of posttranslational regulation of eukaryotic myosins from different classes across species by allosteric intrinsic and extrinsic effectors. First, we highlight the impact of heavy and light chain phosphorylation. Second, we outline intramolecular regulatory mechanisms such as autoinhibition and subsequent activation. Third, we discuss diverse extramolecular allosteric mechanisms ranging from actin-linked regulatory mechanisms to myosin:cargo interactions. At last, we briefly outline the allosteric regulation of myosins with synthetic compounds.

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Section: Figmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Various Themes of Myosin Regulation

Heissler

Sellers

2016

Journal of Molecular Biology

117

127

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“…Although Ahsg was significantly lower in the 4L and 4H groups, the growth of the fish and the expression of immune defense genes in the groups were not significantly different from those of the control group. A myosin type was also altered in the algal groups-myosins are motor proteins that bind to actin, and they convert chemical energy into mechanical work, which enables them to move along actin filaments (Heissler and Sellers, 2016). My11 heavy chain is expressed in the smooth muscle cells of the gastrointestinal tract of mammals, and the expression of the protein was unchanged by hypertrophy (Park et al, 2015), which is associated with inflammation (Blennerhassett et al, 1992).…”

Section: Health Status Upon Feeding Desmodesmus To Atlantic Salmonmentioning

confidence: 99%

Defatted Biomass of the Microalga, Desmodesmus sp., Can Replace Fishmeal in the Feeds for Atlantic salmon

et al. 2016

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Microalgal biomass is a potential feed ingredient that can replace fishmeal and ensure sustainability standards in aquaculture. To understand the efficacy of the defatted biomass from the marine microalga, Desmodesmus sp. a 70-day feeding study was performed with Atlantic salmon (Salmo salar) smolts. Three groups of fish (av. wt. 167 g) were offered either a control feed (without the microalga) or the microalga-containing (10/20%) feeds. At the end of the feeding period, the growth indices (condition factor, specific growth rate) and survival of the microalga-fed fish were not significantly different from the respective values of the control fish, but the feed conversion ratios were inferior. The proximate composition of the whole body of salmon from the three groups did not vary significantly. Compared to the control fish, the 10% alga-fed fish had lower lipid content in their filet. The protein and lipid digestibility in the three feeds did not differ significantly, but the digestibility of energy in the 10% alga-feed was significantly lower than that of the control feed. Furthermore, comparison of the distal intestinal proteome of Atlantic salmon revealed that the expressions of Alpha-2-HS-glycoprotein-like (Ahsg), Myosin-11 isoform X1 (My11) and Dihydrolipoyl dehydrogenase, mitochondrial-like (Dld) were altered by the microalgal feeding. Examination of the physiological status of the fish based on the serum antioxidant capacities did not reveal any alga-feed-related differences. Moreover, the expression of the selected immune and inflammatory marker genes and the micromorphological observations did not indicate any aberration in the intestinal health of the microalga-fed fish. It is possible to include 20% of defatted Desmodesmus sp. in the feeds of Atlantic salmon.

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“…Myosins constitute a superfamily of ubiquitous, multifunctional and structurally related motor proteins that catalyze the hydrolysis of ATP to power the directed movement on filamentous actin. Members of the ∼31 myosin classes participate in all aspects of eukaryotic physiology, from the contraction of muscle, the transport of organelles, the generation of cytoskeletal tension to the function of the mitotic spindle, and autophagy .…”

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confidence: 99%

Kinetic Adaptations of Myosins for Their Diverse Cellular Functions

Heissler

Sellers

2016

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Members of the myosin superfamily are involved in all aspects of eukaryotic life. Their function ranges from the transport of organelles and cargos to the generation of membrane tension, and the contraction of muscle. The diversity of physiological functions is remarkable, given that all enzymatically active myosins follow a conserved mechanoenzymatic cycle in which the hydrolysis of ATP to ADP and inorganic phosphate is coupled to either actin-based transport or tethering of actin to defined cellular compartments. Kinetic capacities and limitations of a myosin are determined by the extent to with actin can accelerate the hydrolysis of ATP and the release of the hydrolysis products and are indispensably linked to its physiological tasks. This review focuses on kinetic competencies that – together with structural adaptations – result in myosins with unique mechanoenzymatic properties targeted to their diverse cellular function.

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Myosins

Cited by 8 publications

References 109 publications

Various Themes of Myosin Regulation

Various Themes of Myosin Regulation

Defatted Biomass of the Microalga, Desmodesmus sp., Can Replace Fishmeal in the Feeds for Atlantic salmon

Kinetic Adaptations of Myosins for Their Diverse Cellular Functions

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