Mechanical proteins

Physics ◽  
2010 ◽  
Vol 3 ◽  
Author(s):  
Anonymous
Keyword(s):  
Mechanical Proteins

scholarly journals Molecular Machinery and Pathophysiology of Mitochondrial Dynamics

2021 ◽  
Vol 9 ◽  
Author(s):  
Yi-Han Chiu ◽  
Shu-Chuan Amy Lin ◽  
Chen-Hsin Kuo ◽  
Chia-Jung Li
Keyword(s):  
Molecular Mechanisms ◽  
Mitochondrial Dynamics ◽  
Biological Significance ◽  
Lipid Synthesis ◽  
Mitochondrial Morphology ◽  
Animal Cells ◽  
Main Site ◽  
Mechanical Proteins ◽  
Molecular Machinery ◽  
Active Processes

Mitochondria are double-membraned organelles that exhibit fluidity. They are the main site of cellular aerobic respiration, providing energy for cell proliferation, migration, and survival; hence, they are called “powerhouses.” Mitochondria play an important role in biological processes such as cell death, cell senescence, autophagy, lipid synthesis, calcium homeostasis, and iron balance. Fission and fusion are active processes that require many specialized proteins, including mechanical enzymes that physically alter mitochondrial membranes, and interface proteins that regulate the interaction of these mechanical proteins with organelles. This review discusses the molecular mechanisms of mitochondrial fusion, fission, and physiopathology, emphasizing the biological significance of mitochondrial morphology and dynamics. In particular, the regulatory mechanisms of mitochondria-related genes and proteins in animal cells are discussed, as well as research trends in mitochondrial dynamics, providing a theoretical reference for future mitochondrial research.

scholarly journals Mitochondrial fission and fusion

2010 ◽  
Vol 47 ◽  
pp. 85-98 ◽  
Author(s):  
Iain Scott ◽  
Richard J. Youle
Keyword(s):  
Mitochondrial Fission ◽  
Adaptor Proteins ◽  
Cell Types ◽  
Mitochondrial Morphology ◽  
Mitochondrial Membranes ◽  
Mechanical Proteins ◽  
A Cell ◽  
Active Processes ◽  
Organelle Morphology ◽  
Cellular Organelles

Mitochondria are highly dynamic cellular organelles, with the ability to change size, shape and position over the course of a few seconds. Many of these changes are related to the ability of mitochondria to undergo the highly co-ordinated processes of fission (division of a single organelle into two or more independent structures) or fusion (the opposing reaction). These actions occur simultaneously and continuously in many cell types, and the balance between them regulates the overall morphology of mitochondria within any given cell. Fission and fusion are active processes which require many specialized proteins, including mechanical enzymes that physically alter mitochondrial membranes, and adaptor proteins that regulate the interaction of these mechanical proteins with organelles. Although not fully understood, alterations in mitochondrial morphology appear to be involved in several activities that are crucial to the health of cells. In the present chapter we discuss the mechanisms behind mitochondrial fission and fusion, and discuss the implications of changes in organelle morphology during the life of a cell.

scholarly journals Nanomechanical phenotypes in cMyBP-C mutants that cause hypertrophic cardiomyopathy

2020 ◽  
Author(s):  
Carmen Suay-Corredera ◽  
Maria Rosaria Pricolo ◽  
Diana Velázquez-Carreras ◽  
Carolina Pimenta-Lopes ◽  
David Sánchez-Ortiz ◽  
...  
Keyword(s):  
Hypertrophic Cardiomyopathy ◽  
Single Molecule ◽  
Molecular Motor ◽  
Sarcomeric Proteins ◽  
Wild Type ◽  
Pathogenic Variants ◽  
Atomic Force ◽  
Myosin Binding Protein ◽  
Myosin Binding Protein C ◽  
Mechanical Proteins

ABSTRACTHypertrophic cardiomyopathy (HCM) is a disease of the myocardium caused by mutations in sarcomeric proteins with mechanical roles, such as the molecular motor myosin. Around half of the HCM-causing genetic variants target contraction modulator cardiac myosin-binding protein C (cMyBP-C), although the underlying pathogenic mechanisms remain unclear since many of these mutations cause no alterations in protein structure and stability. As an alternative pathomechanism, here we have examined whether pathogenic mutations perturb the nanomechanics of cMyBP-C, which would compromise its modulatory mechanical tethers across sliding actomyosin filaments. Using single-molecule atomic force spectroscopy, we have quantified mechanical folding and unfolding transitions in cMyBP-C mutant domains. Our results show that domains containing mutation R495W are mechanically weaker than wild-type at forces below 40 pN, and that R502Q mutant domains fold faster than wild-type. None of these alterations are found in control, non-pathogenic variants, suggesting that nanomechanical phenotypes induced by pathogenic cMyBP-C mutations contribute to HCM development. We propose that mutation-induced nanomechanical alterations may be common in mechanical proteins involved in human pathologies.

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