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J. Biol. Chem., Vol. 278, Issue 1, 208-218, January 3, 2003
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From the Tetraspanins associate on the cell membrane with
several transmembrane proteins, including members of the integrin
superfamily. The tetraspanin CD9 has been implicated in cell motility,
metastasis, and sperm-egg fusion. In this study we characterize the
first CD9 conformation-dependent epitope (detected by
monoclonal antibody (mAb) PAINS-13) whose expression depends on changes
in the activation state of associated
A Functionally Relevant Conformational Epitope on the CD9
Tetraspanin Depends on the Association with Activated
1
Integrin*
§,,
,,,§§¶¶
Instituto de Farmacología y
Toxicología CSIC-UCM, Facultad de Medicina, Universidad
Complutense, 28040 Madrid, Spain, the ¶ Servicio de
Inmunología, Hospital de la Princesa, 28006 Madrid, Spain,
** INSERM U268, Hôpital Paul Brousse, Villejuif, 94807 France, the Departamento de
Bioquímica y Biología Molecular, Facultad de
Ciencias Químicas, Universidad Complutense, 28040 Madrid,
Spain, and the §§ Departamento de
Bioquímica, Facultad de Medicina, Universidad Autónoma de
Madrid, 28029 Madrid, Spain
1 integrins.
MAb PAINS-13 precipitates CD9 under conditions that preserve the
association of this tetraspanin with integrins, but not under
conditions that disrupt these interactions. Induction of activation of
1 integrins by temperature, divalent cation
Mn2+, or mAb TS2/16 correlated with enhanced expression of
the PAINS-13 epitope on a variety of cells. Through the use of
different K562 myeloid leukemia transfectant cells expressing specific
members of the 1 integrin subfamily we show that the
expression of the PAINS-13 epitope depends on CD9 association with
61 integrin. The mAb PAINS-13 reactivity
has been mapped to the CD9 region comprising residues 112-154 in the
NH2 half of the large extracellular loop. Also, we
show that the CD9 conformation recognized by mAb PAINS-13 is
functionally relevant in 1 integrin-mediated cellular processes including wound healing migration, tubular morphogenesis, cell adhesion and spreading and in signal transduction involving phosphatidylinositol 3-kinase activation.
*
This work was supported in part by a grant from Ministerio
de Ciencia y Tecnología CICYT SAF 2001-2807 and a grant from
Ministerio de Sanidad y Consumo FIS-01/1367 (to C. C.).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.
Recipient of a Formación de Profesorado
Universitario predoctoral fellowship from Ministerio de
Educación, Cultura y Deporte.
¶¶
To whom correspondence should be addressed: Instituto
de Farmacología y Toxicología (CSIC-UCM), Facultad de
Medicina UCM, Pabellón III, 28040 Madrid, Spain. Tel.:
34-91-3941444; Fax: 34-91-3941470; E-mail: cacabagu@med.ucm.es.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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