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Molecular and Cellular Biology, May 2002, p. 3527-3536, Vol. 22, No. 10
0270-7306/02/$04.00+0     DOI: 10.1128/MCB.22.10.3527-3536.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Tyrosine Phosphorylation Regulates Alpha II Spectrin Cleavage by Calpain

Gaël Nicolas,1 Catherine M. Fournier,1 Colette Galand,1 Laurence Malbert-Colas,1 Odile Bournier,1 Yolande Kroviarski,1 Monique Bourgeois,1 Jacques H. Camonis,2 Didier Dhermy,1 Bernard Grandchamp,1 and Marie-Christine Lecomte1*

INSERM U409, Faculté de Médecine Xavier Bichat-Association Claude Bernard,1 INSERM U248, Institut Curie, Paris, France2

Received 26 November 2001/ Accepted 1 February 2002

Spectrins, components of the membrane skeleton, are implicated in various cellular functions. Understanding the diversity of these functions requires better characterization of the interacting domains of spectrins, such as the SH3 domain. Yeast two-hybrid screening of a kidney cDNA library revealed that the SH3 domain of {alpha}II-spectrin binds specifically isoform A of low-molecular-weight phosphotyrosine phosphatase (LMW-PTP). The {alpha}II-spectrin SH3 domain does not interact with LMW-PTP B or C nor does LMW-PTP A interact with the {alpha}I-spectrin SH3 domain. The interaction of spectrin with LMW-PTP A led us to look for a tyrosine-phosphorylated residue in {alpha}II-spectrin. Western blotting showed that {alpha}II-spectrin is tyrosine phosphorylated in vivo. Using mutagenesis on recombinant peptides, we identified the residue Y1176 located in the calpain cleavage site of {alpha}II-spectrin, near the SH3 domain, as an in vitro substrate for Src kinase and LMW-PTP A. This Y1176 residue is also an in vivo target for kinases and phosphatases in COS cells. Phosphorylation of this residue decreases spectrin sensitivity to calpain in vitro. Similarly, the presence of phosphatase inhibitors in cell culture is associated with the absence of spectrin cleavage products. This suggests that the Y1176 phosphorylation state could modulate spectrin cleavage by calpain and may play an important role during membrane skeleton remodeling.

* Corresponding author. Mailing address: INSERM 409, Faculté de Médecine Xavier Bichat, 16 rue Henri Huchard, BP416, 75870 Paris Cedex 18, France. Phone: (33) 01 44 85 63 45. Fax: (33) (1) 01 42 26 46 24. E-mail: lecomte{at}bichat.inserm.fr.

Molecular and Cellular Biology, May 2002, p. 3527-3536, Vol. 22, No. 10
0022-538X/02/$04.00+0     DOI: 10.1128/MCB.22.10.3527-3536.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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