Post-translational modifications and stabilization of microtubules regulate transport of viral factors during infections

被引:4
|
作者
Requena, Silvia [1 ]
Sanchez-Madrid, Francisco [1 ,2 ,3 ]
Martin-Cofreces, Noa B. [1 ,2 ,3 ]
机构
[1] UAM, Immunol Serv, IIS IP, Hosp Univ Princesa, Madrid 28006, Spain
[2] Ctr Invest Biomed Red Enfermedades Cardiovasc CIB, Campus Sinesio Delgado, Madrid 28029, Spain
[3] Fdn Ctr Nacl Invest Cardiovasc Carlos III, Lab Intercellular Commun, Area Vasc Pathophysiol, Madrid 28029, Spain
关键词
TUBULIN CYTOSKELETON; MOLECULAR-BASIS; PLUS-END; DYNAMICS; HDAC6; DYNEIN; ACETYLATION; PROTEINS; ACTIN; PHOSPHORYLATION;
D O I
10.1042/BST20210017
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Tubulin post-translational modifications (PTMs) constitute a source of diversity for microtubule (MT) functions, in addition to the different isotypes of alpha and beta-tubulin acting as building blocks of MTs. Also, MT-associated proteins (MAPs) confer different characteristics to MTs. The combination of all these factors regulates the stability of these structures that act as rails to transport organelles within the cell, facilitating the association of motor complexes. All these functions are involved in crucial cellular processes in most cell types, ranging from spindle formation in mitosis to the defense against incoming cellular threats during phagocytosis mediated by immune cells. The regulation of MT dynamics through tubulin PTMs has evolved to depend on many different factors that act in a complex orchestrated manner. These tightly regulated processes are particularly relevant during the induction of effective immune responses against pathogens. Viruses have proved not only to hijack MTs and MAPs in order to favor an efficient infection, but also to induce certain PTMs that improve their cellular spread and lead to secondary consequences of viral processes. In this review, we offer a perspective on relevant MT-related elements exploited by viruses.
引用
收藏
页码:1735 / 1748
页数:14
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