Short Communication - Journal of Cell Biology and Metabolism (2023) Volume 5, Issue 2

An interaction between genetics and mechanics in mitochondrial function

Department of Cell Biology, Utrecht University, Padualaan, Netherlands

*Corresponding Author:

Anna matty
Department of Cell Biology
Utrecht University, Padualaan, Netherlands
E-mail: annamatty@edu.com

Received: 28-Mar-2023, Manuscript No. AACBM-23-59205; Editor assigned: 30-Mar-2023, PreQC No. AACBM-23-59205 (PQ); Reviewed: 13-Apr-2023, QC No AACBM -23- 59205; Revised: 18-Apr-2023, Manuscript No. AACBM -23-59205 (R); Published: 25-Apr-2023, DOI:10.35841/aacbm-5.2.136

Citation: Matty A. An interaction between genetics and mechanics in mitochondrial function. J Cell Biol Metab. 2022;5(2):136

Introduction

Chromosome segregation and intracellular structure depend on microtubules, which are dynamic polymers of -tubulin. The insertion and deletion of -tubulin subunits are biological processes that cause microtubule growth and shrinking. Mechanical actions, such as pushing or tugging against a load, are another way that dynamic microtubules can produce forces. The presence of different tubulin conformations and their crucial function in determining the processes governing microtubule dynamics have recently been established through research at the interface between biochemistry and mechanics. In order to control microtubule dynamics, proteins associated with microtubules specifically target particular tubulin conformations. Mechanical forces can also have an impact on microtubule dynamics by changing the balance of tubulin conformations. It's significant because the conformational states of tubulin dimers appear to be connected across the lattice, meaning that one dimer's conformation influences its immediate neighbours' conformation and beyond. This linkage offers a long-range method through which MAPs and forces can control the expansion and contraction of microtubules. These studies demonstrate that microtubule cellular activities depend on the interaction of biochemistry and mechanics [1].

The cytoskeleton of eukaryotic cells is made up of long, rigid polymers of -tubulin called microtubules. These microtubules create the mitotic spindle, the axonemes of cilia and flagella, and act as tracks for intracellular trafficking. The microtubule end, where a "stabilizing cap" forms because GTP hydrolysis takes time to occur, is where they expand by adding GTPtubulin dimers. Its GTP-tubulin-enriched cap attracts "endbinding" proteins as well as a variety of other microtubuleassociated proteins (MAPs), such as kinesins and microtubule polymerases and depolymerases, which collaborate and compete to determine the fate of the microtubule. On rare occasions, a microtubule that is quickly contracting is "rescued," turning from contraction to growth. Cells can use this dynamic instability, or switching behaviour, to impose pressures, such as during chromosome segregation in mitosis [2].

Microtubules exhibit close interactions between biochemical and mechanical processes, including fast turnover, dynamic instability, and the stiffness of a stiff polymer 8. Microtubules can be seen from many angles thanks to the interaction between biology and mechanics. Microtubules are seen from a biochemical standpoint as a group of distinct subunits 9 that create a lattice with two basic mechanisms of interaction. The behavior of the stabilizing cap just before a catastrophe and the stochastic length variations that take place during elongation have been characterized thanks to recent advancements in single-molecule imaging, which enable microtubule growth to be watched with a resolution of 40 nm. These recent observations reveal fresh information about the biology behind microtubule motion. Microtubules, on the other hand, are seen as a continuous substance from a mechanical standpoint. Microtubule rigidity is equivalent to that of plexiglass, according to groundbreaking measurements, in fact [3].

Since that mechanical phenomena act at the level of different subunits, it is obvious that the boundary between biochemical and mechanical views is artificial9. GTP-tubulin binds to the microtubule end in the tubulin biochemical cycle, hydrolyzes the GTP and releases phosphate while in the lattice, and subsequently dissociates from the microtubule as GDP-tubulin. The case for mechanical rather than chemical alterations in tubulin conformation accompanying this metabolic cycle will be advanced in this review. Many different oligomeric proteins take use of the conformational changes brought on by nucleotide hydrolysis to do mechanical labour. The structural complexity of the expanding and decreasing ends of microtubules, we shall contend, gives them a special quality. In the first section, we go over the dynamics of the microtubule end and present evidence for the many conformations that tubulin dimers at the growing end can take in response to the biochemical cycle of GTP hydrolysis [4].

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