Myosin XIX

Bocanegra, Jennifer L.; Adikes, Rebecca C.; Quintero, Omar A.

doi:10.1007/978-3-030-38062-5_20

Cited by 4 publications

(6 citation statements)

References 49 publications

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“…By using the actin cytoskeleton as tracks, myosin also powers cellular cargo transport processes and can serve as a molecular anchor and force sensor ( Hartman et al, 2011 ; Woolner and Bement, 2009 ). Due to its versatility, myosin is key to numerous essential cellular processes including cytokinesis, transcription, signal transduction, cell migration and adhesion, and endo- and exocytosis ( Coluccio, 2020 ; Krendel and Mooseker, 2005 ). While this variety in functions is well reflected by the diversity of the myosin superfamily ( Sellers, 2000 ), the ATP-dependent force generation mechanism as well as the architecture of the motor domain is shared by all myosins ( Cope et al, 1996 ).…”

Section: Introductionmentioning

confidence: 99%

“…Decades of biochemical studies have brought great insights into the diversity and kinetics of the myosin superfamily ( Coluccio, 2020 ; Geeves et al, 2005 ). However, detailed structural information is ultimately required to understand the mechanism of force generation.…”

Section: Introductionmentioning

confidence: 99%

“…Therefore, they are best suited to structurally study actin-bound states other than the rigor. Today, class V and VI myosins are probably the best-characterized unconventional myosins, both structurally and biochemically ( Coluccio, 2020 ). Cryo-EM studies of actomyosin-V have further reported structures of the strong-ADP and rigor state ( Wulf et al, 2016 ), as well as a potential PPS transition state ( Volkmann et al, 2005 ).…”

Section: Introductionmentioning

confidence: 99%

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High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism

Pospich

Sweeney

Houdusse

et al. 2021

eLife

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The molecular motor myosin undergoes a series of major structural transitions during its force-producing motor cycle. The underlying mechanism and its coupling to ATP hydrolysis and actin binding is only partially understood, mostly due to sparse structural data on actin-bound states of myosin. Here, we report 26 high-resolution cryo-EM structures of the actomyosin-V complex in the strong-ADP, rigor, and a previously unseen post-rigor transition state that binds the ATP analog AppNHp. The structures reveal a high flexibility of myosin in each state and provide valuable insights into the structural transitions of myosin-V upon ADP release and binding of AppNHp, as well as the actomyosin interface. In addition, they show how myosin is able to specifically alter the structure of F-actin.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism

Pospich

Sweeney

Houdusse

et al. 2021

eLife

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“…To satisfy the increased energy demands, increased mitochondrial biogenesis and elevated electron transport chain (ECT) efficiency are adopted for skeletal muscle cells. Two individual RNA sequencing studies detected significantly upregulated Myo19 mRNA level in young human males and thoroughbred horses after high intensity training 60 – 62 . Concerning our finding that Myo19 affects mitochondria metabolism, it is likely that Myo19 may contribute to skeletal muscle energy demands.…”

Section: Discussionmentioning

confidence: 99%

“…Metabolic switch from OXPHOS to glycolysis, known as Warburg effect, is a hallmark of cancer, supporting tumor growth and cancer stemness. Genome-wide association studies suggest that Myo19 may involve in ovarian cancer, pancreatic ductal adenocarcinoma and breast cancer but whether it may play a tumor suppressive role is unclear 62 – 67 . In Myo19 deleted MDA-MB-231 breast cancer cells, we detected decreased maximal OCR and a little increased basal ECAR, showing a tilted metabolic balance.…”

Section: Discussionmentioning

confidence: 99%

Mechanical instability generated by Myosin 19 contributes to mitochondria cristae architecture and OXPHOS

et al. 2022

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The folded mitochondria inner membrane-cristae is the structural foundation for oxidative phosphorylation (OXPHOS) and energy production. By mechanically simulating mitochondria morphogenesis, we speculate that efficient sculpting of the cristae is organelle non-autonomous. It has long been inferred that folding requires buckling in living systems. However, the tethering force for cristae formation and regulation has not been identified. Combining electron tomography, proteomics strategies, super resolution live cell imaging and mathematical modeling, we reveal that the mitochondria localized actin motor-myosin 19 (Myo19) is critical for maintaining cristae structure, by associating with the SAM-MICOS super complex. We discover that depletion of Myo19 or disruption of its motor activity leads to altered mitochondria membrane potential and decreased OXPHOS. We propose that Myo19 may act as a mechanical tether for effective ridging of the mitochondria cristae, thus sustaining the energy homeostasis essential for various cellular functions.

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Regulation of mitochondrial structure by the actin cytoskeleton

Wu,

Ren,

Shi

et al. 2023

Cytoskeleton

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Mitochondria are the powerhouse of the cell and play important roles in multiple cellular processes including cell metabolism, proliferation, and programmed cell death. Mitochondria are double‐membrane organelles with the inner membrane folding inward to form cristae. Mitochondria networks undergo dynamic fission and fusion. Deregulation of mitochondrial structure has been linked to perturbed mitochondrial membrane potential and disrupted metabolism, as evidenced in tumorigenesis, neurodegenerative diseases, etc. Actin and its motors‐myosins have long been known to generate mechanical forces and participate in short‐distance cargo transport. Accumulating knowledge from biochemistry and live cell/electron microscope imaging has demonstrated the role of actin filaments in pre‐constricting the mitochondria during fission. Recent studies have suggested the involvement of myosins in cristae maintenance and mitochondria quality control. Here, we review current findings and discuss future directions in the emerging fields of cytoskeletal regulation in cristae formation, mitochondrial dynamics, intracellular transport, and mitocytosis, with focus on the actin cytoskeleton and its motor proteins.

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Myosin XIX

Cited by 4 publications

References 49 publications

High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism

High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism

Mechanical instability generated by Myosin 19 contributes to mitochondria cristae architecture and OXPHOS

Regulation of mitochondrial structure by the actin cytoskeleton

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