The Kinetic Mechanism of Mouse Myosin VIIA

Haithcock, Jessica; Billington, Neil; Choi, Kevin; Fordham, Jennifer; Sellers, James R.; Stafford, Walter F.; White, Howard D.; Forgács, Éva

doi:10.1074/jbc.m110.163592

Cited by 23 publications

(33 citation statements)

References 52 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Its high duty ratio allows Myo7A to act as a processive motor when dimerized (Watanabe et al, 2006;Yang et al, 2006;Haithcock et al, 2011). Myo7A is thought to dimerize with the help of factors binding to its tail region (Yang et al, 2009;Umeki et al, 2009;Haithcock et al, 2011). The highduty processive motor activity of Myo7A is consistent with a function in transporting cargo or in anchoring plasma membrane components to the actin bundle to generate tension forces (reviewed by El-Amraoui et al, 2008).…”

Section: Introductionmentioning

confidence: 83%

“…Once activated, Myo7A appears to be predominantly locked in an ADP-bound state, in which it strongly binds to actin. Its high duty ratio allows Myo7A to act as a processive motor when dimerized (Watanabe et al, 2006;Yang et al, 2006;Haithcock et al, 2011). Myo7A is thought to dimerize with the help of factors binding to its tail region (Yang et al, 2009;Umeki et al, 2009;Haithcock et al, 2011).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Myosin VIIA regulates microvillus morphogenesis and interacts with cadherin Cad99C in Drosophila oogenesis

Glowinski

Liu

Chen

et al. 2014

Journal of Cell Science

View full text Add to dashboard Cite

BSTRACTMicrovilli and related actin-based protrusions permit multiple interactions between cells and their environment. How the shape, length and arrangement of microvilli are determined remains largely unclear. To address this issue and explore the cooperation of the two main components of a microvillus, the central F-actin bundle and the enveloping plasma membrane, we investigated the expression and function of Myosin VIIA (Myo7A), which is encoded by crinkled (ck), and its interaction with cadherin Cad99C in the microvilli of the Drosophila follicular epithelium. Myo7A is present in the microvilli and terminal web of follicle cells, and associates with several other F-actin-rich structures in the ovary. Loss of Myo7A caused brush border defects and a reduction in the amount of the microvillus regulator Cad99C. We show that Myo7A and Cad99C form a molecular complex and that the cytoplasmic tail of Cad99C recruits Myo7A to microvilli. Our data indicate that Myo7A regulates the structure and spacing of microvilli, and interacts with Cad99C in vivo. A comparison of the mutant phenotypes suggests that Myo7A and Cad99C have co-dependent and independent functions in microvilli.

show abstract

Section: Introductionmentioning

confidence: 83%

Section: Introductionmentioning

confidence: 99%

Myosin VIIA regulates microvillus morphogenesis and interacts with cadherin Cad99C in Drosophila oogenesis

Glowinski

Liu

Chen

et al. 2014

Journal of Cell Science

View full text Add to dashboard Cite

show abstract

“…Myosin‐7A is a monomeric high duty ratio motor that is important for the maintenance and development of actin‐based protrusions such as filopodia and stereocilia . It is implicated in the transport and localization of the Usher I scaffold proteins harmonin and sans that are important for hearing and vision .…”

Section: Autoinhibitionmentioning

confidence: 99%

Kinetic Adaptations of Myosins for Their Diverse Cellular Functions

Heissler

Sellers

2016

Traffic

Self Cite

View full text Add to dashboard Cite

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.

show abstract

“…Drosophila Myo7a can form an inactive monomer regulated by head-to-tail folding 82 but appears to function as a processive dimer 83 , 84 . Biochemical experiments indicate Myo7a has a high duty ratio 85 , 86 . In mammals, Myo7a is predominantly expressed in epithelial cells 87 with highest levels in the testis, cochlea and retina and lower expression in kidney 88 …”

Section: Myosin-viia Interacts With Junction-associated Proteins At Ementioning

confidence: 99%

Myosins in cell junctions

Liu¹,

Cheney²

2012

BioArchitecture

View full text Add to dashboard Cite

The development of cell-cell junctions was a fundamental step in metazoan evolution, and human health depends on the formation and function of cell junctions. Although it has long been known that actin and conventional myosin have important roles in cell junctions, research has begun to reveal the specific functions of the different forms of conventional myosin. Exciting new data also reveals that a growing number of unconventional myosins have important roles in cell junctions. Experiments showing that cell junctions act as mechanosensors have also provided new impetus to understand the functions of myosins and the forces they exert. In this review we will summarize recent developments on the roles of myosins in cell junctions.

show abstract

The Kinetic Mechanism of Mouse Myosin VIIA

Cited by 23 publications

References 52 publications

Myosin VIIA regulates microvillus morphogenesis and interacts with cadherin Cad99C in Drosophila oogenesis

Myosin VIIA regulates microvillus morphogenesis and interacts with cadherin Cad99C in Drosophila oogenesis

Kinetic Adaptations of Myosins for Their Diverse Cellular Functions

Myosins in cell junctions

Contact Info

Product

Resources

About