Calcium gets myosin VI ready for work

Masters, Thomas A.; Kendrick‐Jones, John; Buß, Folma

doi:10.1073/pnas.1600725113

Cited by 3 publications

(1 citation statement)

References 19 publications

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“…There are at least 18 classes of myosin proteins identified in the animal and plant kingdoms (Thompson & Langford, 2002). The human genome encodes 12 different classes of myosins, and each one is designated for different cellular functions (Heissler & Sellers, 2014, Masters et al, 2016. Myosin in striated muscles (skeletal and cardiac muscles) are class II myosins ( Figure 1.4 A), a hexameric protein complex with two heavy chains and two pairs of light chains (Cooper, 2000).…”

Section: Troponin and Tropomyosinmentioning

confidence: 99%

Electron tomography of muscle cross- bridge by regulatory light chain labelling with APEX2

Mufeeda¹

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Section: Troponin and Tropomyosinmentioning

confidence: 99%

Electron tomography of muscle cross- bridge by regulatory light chain labelling with APEX2

Mufeeda¹

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Dissecting Pistil Responses to Incompatible and Compatible Pollen in Self-Incompatibility Brassica oleracea Using Comparative Proteomics

et al. 2017

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Angiosperms have developed self-incompatibility (SI) systems to reject self-pollen, thereby promoting outcrossing. The Brassicaceae belongs to typical sporophytic system, having a single S-locus controlled SI response, and was chosen as a model system to study SI-related intercellular signal transduction. In this regard, the downstream factor of EXO70A1 was unknown. Here, protein two-dimensional electrophoresis (2-DE) method and coupled with matrix-assisted laser desorption ionization/time of flight of flight mass spectrometry (MALDI-TOF -MS) and peptide mass fingerprinting (PMF) was used to further explore the mechanism of SI responses in Brassica oleracea L. var. capitata L. at protein level. To further confirm the time point of protein profile change, total proteins were collected from B. oleracea pistils at 0 min, 1 h, and 2 h after self-pollination. In total 902, 1088 and 1023 protein spots were separated in 0 min, 1 h and 2 h 2-DE maps, respectively. Our analyses of self-pollination profiles indicated that proteins mainly changed at 1 h post-pollination in B. oleracea. Moreover, 1077 protein spots were separated in cross-pollinated 1 h (CP) pistil 2-DE map. MALDI-TOF-MS and PMF successfully identified 34 differentially-expressed proteins (DEPs) in SP and CP 1 h 2-DE maps. Gene ontology and KEGG analysis revealed an array of proteins grouped in the following categories: stress and defense response (35%), protein metabolism (18%), carbohydrate and energy metabolism (12%), regulation of translation (9%), pollen tube development (12%), transport (9%) and cytoskeletal (6%). Sets of DEPs identified specifically in SP or only up-regulated expressed in CP pistils were chosen for funther investigating in floral organs and during the process of self- and cross-pollination. The function of these DEPs in terms of their potential involvement in SI in B. oleracea is discussed.

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Motor domain phosphorylation increases nucleotide exchange and turns MYO6 into a faster and stronger motor

de Jonge,

Graw,

Kargas

et al. 2024

Nat Commun

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Myosin motors perform many fundamental functions in eukaryotic cells by providing force generation, transport or tethering capacity. Motor activity control within the cell involves on/off switches, however, few examples are known of how myosins regulate speed or processivity and fine-tune their activity to a specific cellular task. Here, we describe a phosphorylation event for myosins of class VI (MYO6) in the motor domain, which accelerates its ATPase activity leading to a 4-fold increase in motor speed determined by actin-gliding assays, single molecule mechanics and stopped flow kinetics. We demonstrate that the serine/threonine kinase DYRK2 phosphorylates MYO6 at S267 in vitro. Single-molecule optical-tweezers studies at low load reveal that S267-phosphorylation results in faster nucleotide-exchange kinetics without change in the working stroke of the motor. The selective increase in stiffness of the acto-MYO6 complex when proceeding load-dependently into the nucleotide-free rigor state demonstrates that S267-phosphorylation turns MYO6 into a stronger motor. Finally, molecular dynamic simulations of the nucleotide-free motor reveal an alternative interaction network within insert-1 upon phosphorylation, suggesting a molecular mechanism, which regulates insert-1 positioning, turning the S267-phosphorylated MYO6 into a faster motor.

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Calcium gets myosin VI ready for work

Cited by 3 publications

References 19 publications

Electron tomography of muscle cross- bridge by regulatory light chain labelling with APEX2

Electron tomography of muscle cross- bridge by regulatory light chain labelling with APEX2

Dissecting Pistil Responses to Incompatible and Compatible Pollen in Self-Incompatibility Brassica oleracea Using Comparative Proteomics

Motor domain phosphorylation increases nucleotide exchange and turns MYO6 into a faster and stronger motor

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