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Updated: May 26, 2026

Self-Assembly of Microtubule Tactoids
Published on: June 23, 2022
The tau-like protein in silkworm (Bombyx mori) induces microtubule bundle formation
Qiao Wang1, Li Chen, Liang Chen
1The Key Laboratory of Cell Proliferation and Differentiation of Ministry of Education, The State Key Laboratory of Bio-membrane and Membrane Bio-engineering, College of Life Sciences, Peking University, Beijing 100871, China.
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 30 kDa 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.
Insights
Researchers identified a novel tau-like protein, BmTau, in silkworms. This protein functions similarly to its counterparts in bundling microtubules, crucial for neuronal structure.
Area of Science:
- Molecular Biology
- Cell Biology
- Neuroscience
Background:
- Tau proteins are essential microtubule-associated proteins (MAPs) involved in neuronal development and function.
- MAPs regulate microtubule polymerization and spacing within axons of the central and peripheral nervous systems.
Purpose of the Study:
- To clone and characterize a novel tau-like protein from the silkworm, Bombyx mori.
- To investigate the functional role of this protein in microtubule organization.
Main Methods:
- Gene cloning and sequencing of the BmTau protein.
- Quantitative real-time PCR for BmTau expression analysis.
- Immunocytochemical studies using EGFP-tagged BmTau in silkworm cells.
Main Results:
- A tau-like protein, BmTau, was identified with a 723-base coding sequence, encoding a 30 kDa protein.
- BmTau possesses four predicted microtubule-binding domains homologous to Drosophila orthologs.
- Ubiquitous BmTau expression was observed, with high levels in the brain and lower levels in other tissues; BmTau was confirmed to bundle microtubules.
Conclusions:
- BmTau is a functional microtubule-bundling protein, conserved across species.
- The discovery of BmTau provides insights into the evolution and function of tau proteins in invertebrates.
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