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Subcellular distribution of thymosin beta4.

Robert E Zoubek¹, Ewald Hannappel

¹Institute of Biochemistry, University Erlangen-Nuremberg, Fahrstr. 17, Erlangen, Germany. thymosin@biochem.uni-erlangen.de

Annals of the New York Academy of Sciences

|June 15, 2007

Summary

Thymosin beta(4) and its variants distribute equally in living cells but are excluded from the nucleus in depleted cells. Nuclear entry is likely via passive diffusion, not a single transport protein.

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Area of Science:

Cell Biology
Molecular Biology
Protein Localization

Background:

Thymosin beta(4) is a ubiquitous actin-sequestering protein.
Its nuclear localization and transport mechanisms are not fully understood.
Understanding thymosin beta(4) localization is crucial for its cellular functions.

Purpose of the Study:

To investigate the nuclear localization of thymosin beta(4) and its variants.
To determine the role of the basic cluster and actin-binding motif in nuclear transport.
To elucidate the mechanism of thymosin beta(4) nuclear shuttling.

Main Methods:

Oregon Green cadaverine labeling of thymosin beta(4) and variants.
Investigation in cytoplasm-depleted A431 cells.
Microinjection experiments with and without fixation.
Analysis of nuclear pore passage and cellular distribution.

Main Results:

Thymosin beta(4) variants and fragments were excluded from the nucleus in cytoplasm-depleted cells.
All variants showed equal distribution in living cells.
Nuclear localization was independent of actin-binding ability and the basic lysine cluster.
Fragments entered intact nuclei post-injection but were excluded from depleted nuclei.

Conclusions:

Thymosin beta(4) nuclear import is not mediated by a single transport protein.
Passive, regulated diffusion is a likely mechanism for thymosin beta(4) nuclear shuttling.
The basic cluster and actin-binding sites are not essential for nuclear entry.