On and Around Microtubules: An Overview

• Published in: Molecular biotechnology Vol. 43; no. 2; pp. 177 - 191
• Main Author: Wade, Richard H.
• Format: Journal Article
• Language: English
• Published: New York Humana Press Inc 01.10.2009; Springer; Springer Nature B.V
• Subjects: Biochemistry; Biological and medical sciences; Biological Techniques; Biotechnology; Cell Biology; Chemistry; Chemistry and Materials Science; Chromosomes; Crystallography; Cytoskeleton; Fundamental and applied biological sciences. Psychology; Human Genetics; Microtubules - chemistry; Microtubules - physiology; Microtubules - ultrastructure; Models, Biological; Models, Chemical; Models, Molecular; Molecular biology; Molecular Motor Proteins - chemistry; Molecular Motor Proteins - physiology; Molecular Motor Proteins - ultrastructure; Nucleation; Protein Science; Proteins; Review; Structure-Activity Relationship; Studies; Microtubule-associated proteins (MAPs); Tubulin and microtubule structure; Tubulins; Motor proteins; Microtubules; Plus-end tracking proteins (+TIPs); Tubulin; Tubulin and microtubule structures; Motor protein; Microtubule; Structure; Protein; Plus-end tracking proteins (+TIPS)
• ISSN: 1073-6085; 1559-0305
• DOI: 10.1007/s12033-009-9193-5

Microtubules are hollow tubes some 25 nm in diameter participating in the eukaryotic cytoskeleton. They are built from αβ-tubulin heterodimers that associate to form protofilaments running lengthwise along the microtubule wall with the β-tubulin subunit facing the microtubule plus end conferring a structural polarity. The α- and β-tubulins are highly conserved. A third member of the tubulin family, γ-tubulin, plays a role in microtubule nucleation and assembly. Other members of the tubulin family appear to be involved in microtubule nucleation. Microtubule assembly is accompanied by hydrolysis of GTP associated with β-tubulin so that microtubules consist principally of ‘GDP-tubulin’ stabilized at the plus end by a short ‘cap’. An important property of microtubules is dynamic instability characterized by growth randomly interrupted by pauses and shrinkage. Many proteins interact with microtubules within the cell and are involved in essential functions such as microtubule growth, stabilization, destabilization, and interactions with chromosomes during cell division. The motor proteins kinesin and dynein use microtubules as pathways for transport and are also involved in cell division. Crystallography and electron microscopy are providing a structural basis for understanding the interactions of microtubules with antimitotic drugs, with motor proteins and with plus end tracking proteins.