Crystal structure of VASH1-SVBP complex bound with EpoY

Li, Faxiang; Yingjie, Hu,; Qi, Shu-Tao; Luo, Xuelian; Yu, Hongtao

doi:10.2210/pdb6ocg/pdb

2019

DOI: 10.2210/pdb6ocg/pdb

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Crystal structure of VASH1-SVBP complex bound with EpoY

Faxiang Li

Hu, Yingjie

Shu-Tao Qi

et al.

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Cited by 17 publications

References 37 publications

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Posttranslational modifications of the cytoskeleton

MacTaggart

Kashina

2021

Cytoskeleton

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The cytoskeleton plays important roles in many essential processes at the cellular and organismal levels, including cell migration and motility, cell division, and the establishment and maintenance of cell and tissue architecture. In order to facilitate these varied functions, the main cytoskeletal components—microtubules, actin filaments, and intermediate filaments—must form highly diverse intracellular arrays in different subcellular areas and cell types. The question of how this diversity is conferred has been the focus of research for decades. One key mechanism is the addition of posttranslational modifications (PTMs) to the major cytoskeletal proteins. This posttranslational addition of various chemical groups dramatically increases the complexity of the cytoskeletal proteome and helps facilitate major global and local cytoskeletal functions. Cytoskeletal proteins undergo many PTMs, most of which are not well understood. Recent technological advances in proteomics and cell biology have allowed for the in‐depth study of individual PTMs and their functions in the cytoskeleton. Here, we provide an overview of the major PTMs that occur on the main structural components of the three cytoskeletal systems—tubulin, actin, and intermediate filament proteins—and highlight the cellular function of these modifications.

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Posttranslational modifications of the cytoskeleton

MacTaggart

Kashina

2021

Cytoskeleton

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Tubulin post‐translational modifications control neuronal development and functions

Moutin

Bosc

Peris

et al. 2020

Developmental Neurobiology

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Tubulin carboxypeptidase activity of vasohibin-1 inhibits angiogenesis by interfering with endocytosis and trafficking of pro-angiogenic factor receptors

et al. 2020

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Crystal structure of VASH1-SVBP complex bound with EpoY

Cited by 17 publications

References 37 publications

Posttranslational modifications of the cytoskeleton

Posttranslational modifications of the cytoskeleton

Tubulin post‐translational modifications control neuronal development and functions

Tubulin carboxypeptidase activity of vasohibin-1 inhibits angiogenesis by interfering with endocytosis and trafficking of pro-angiogenic factor receptors

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