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J. Biol. Chem., Vol. 276, Issue 48, 44785-44791, November 30, 2001
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From the Centro de Biología Molecular "Severo Ochoa,"
Departamento de Biología Molecular, Facultad de Ciencias,
Universidad Autónoma de Madrid, E-28049 Madrid, Spain
Red blood cell protein 4.1 (4.1R) is an 80-kDa
protein that stabilizes the spectrin-actin network and anchors it to
the plasma membrane. To contribute to the characterization of
functional roles and partners of specific nonerythroid 4.1R isoforms,
we analyzed 4.1R in human T cells and found that endogenous 4.1R was
distributed to the microtubule network. Transfection experiments of T
cell 4.1R cDNAs in conjunction with confocal microscopy analysis revealed the colocalization of exogenous 4.1R isoforms with the tubulin
skeleton. Biochemical analyses using Taxol®
(paclitaxel)-polymerized microtubules from stably transfected T cells
confirmed the association of the exogenous 4.1R proteins with
microtubules. Consistent with this, endogenous 4.1R immunoreactive proteins were also detected in the microtubule-containing fraction. In vitro binding assays using glutathione
S-transferase-4.1R fusion proteins showed that a
constitutive domain of the 4.1R molecule, one that is therefore present
in all 4.1R isoforms, is responsible for the association with tubulin.
A 22-amino acid sequence comprised in this domain and containing
heptad repeats of leucine residues was essential for tubulin binding.
Furthermore, ectopic expression of 4.1R in COS-7 cells provoked
microtubule disorganization. Our results suggest an involvement of 4.1R
in interphase microtubule architecture and support the
hypothesis that some 4.1R functional activities are cell
type-regulated.
4.1R Proteins Associate with Interphase Microtubules in Human
T Cells
A 4.1R CONSTITUTIVE REGION IS INVOLVED IN TUBULIN BINDING*
,
*
This work was supported by Grant PM98-0002 from the
Ministerio de Ciencia y Tecnología, Spain.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Predoctoral fellow of the Ministerio de Educación y Cultura, Spain.
§
Present address: European Molecular Biology Laboratory, D-69117
Heidelberg, Germany.
¶
To whom correspondence should be addressed. Fax:
34-91-397-8087; E-mail: icorreas@cbm.uam.es.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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