IMR Press / FBE / Volume 4 / Issue 3 / DOI: 10.2741/E435

Frontiers in Bioscience-Elite (FBE) is published by IMR Press from Volume 13 Issue 2 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.

Open Access Article

The tau-like protein in silkworm (Bombyx mori) induces microtubule bundle formation

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1 The Key Laboratory of Cell Proliferation and Differentiation of Ministry of Education, The State Key Laboratory of Biomembrane and Membrane Bio-engineering, College of Life Sciences, Peking University, Beijing 100871, China
2 College of Biological and Environmental Engineering, Zhejiang University of Technology, Hangzhou, Zhejiang 310014, China

*Author to whom correspondence should be addressed.

Front. Biosci. (Elite Ed) 2012, 4(3), 998–1008; https://doi.org/10.2741/E435
Published: 1 January 2012
Abstract

Tau proteins are major microtubule-associated proteins (MAPs), which promote polymerization of tubulin and determine spacings between microtubules in axons of both the central and peripheral nervous systems (CNS and PNS). Here, we cloned and identified a tau-like protein BmTau from silkworm, Bombyx mori (GenBank accession number FJ904935). The coding sequence of BmTau is 723 bases long and encodes an approximate 30kDa protein. In the C-terminus of BmTau are contained four predicted microtubule-binding domains, which share strong sequence homology to its ortholog in Drosophila melanoganster. Relative real-time PCR analysis showed ubiquitous expression of BmTau in both neurons and non-neural cells, with its mRNA abundantly expressing in brain but significantly less detected in trachea, fat body, and silkgland. Furthermore, immunocytochemical studies in BmN cells transfected with EGFP-BmTau indicated that BmTau functioned as microtubule bundling protein as its orthologues.

Keywords
Tau
Microtubule-Binding Domain
Microtubule Bundling
Silkworm
Silkgland
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