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Cold-stable and cold-adapted microtubules

M Wallin¹, E Strömberg

¹Department of Zoophysiology, University of Göteborg, Sweden.

International Review of Cytology

|January 1, 1995

Summary

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Microtubules can be stabilized for specific functions using various factors. Cold adaptation in animals suggests intrinsic tubulin properties, not just external factors, are key.

Area of Science:

Cell Biology
Biochemistry
Structural Biology

Background:

Microtubules are essential cytoskeletal components.
Most mammalian microtubules depolymerize at low temperatures.
Some microtubule populations exhibit cold stability for specific cellular functions.

Purpose of the Study:

To explore mechanisms conferring cold stability to microtubules.
To differentiate general microtubule stabilization from cold adaptation in poikilothermic animals.

Main Methods:

Review of existing literature on microtubule stability and cold adaptation.
Analysis of factors influencing microtubule cold stability, including associated proteins and tubulin properties.

Main Results:

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Cold stability can be achieved through microtubule-associated proteins (MAPs), STOPs, histones, capping factors, specific tubulin isotypes, and posttranslational modifications.
Permanent stabilization involves bundling factors, membrane associations, and microtubule doublet/triplet assembly.
Cold adaptation in poikilothermic animals appears intrinsic to tubulin, potentially involving amino acid sequence or posttranslational modifications.

Conclusions:

Microtubule cold stability is multifactorial, involving both intrinsic tubulin properties and extrinsic factors.
Cold adaptation in animals suggests inherent tubulin characteristics are crucial for function at low temperatures.
Further research is needed to elucidate the precise molecular basis of tubulin-dependent cold adaptation.