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The dystroglycan adhesion complex consists of two noncovalently interact-ing proteins: a-dystroglycan, a peripheral extracellular subunit that is extensively glycosylated, and the transmembrane b-dystroglycan, whose cytosolic tail interacts with dystrophin, thus linking the F-actin cytoskele-ton to the extracellular matrix. | ỊFEBS Journal Concerted mutation of Phe residues belonging to the b-dystroglycan ectodomain strongly inhibits the interaction with a-dystroglycan in vitro UH I I 1 I- 2 1 t 7 1 -3 1 . I-V 2 Manuela Bozzi Francesca Sciandra Lorenzo Ferri Paola Torreri Ernesto Pavoni Tamara C. Petrucci3 Bruno Giardina2 and Andrea Brancaccio2 1 Istituto di Biochimica e Biochimica Clinica Universita Cattolica delSacro Cuore Rome Italy 2 CNR Istituto di Chimica delRiconoscimento Molecolare c o Istituto di Biochimica e Biochimica Clinica Universita Cattolica delSacro Cuore Rome Italy 3 Dipartimento di Biologia Cellulare e Neuroscienze Istituto Superiore di Sanita Rome Italy Keywords alanine scanning cell transfection dystroglycan protein-protein interaction site-directed mutagenesis Correspondence A. Brancaccio CNR Istituto di Chimica del Riconoscimento Molecolare c o Istituto di Biochimica e Biochimica Clinica Universita Cattolica delSacro Cuore Largo Francesco Vito 1 00168 Rome Italy Fax 39 6 3053598 Tel 39 6 3057612 E-mail andrea.brancaccio@icrm.cnr.it These authors contributed equally to this work Received 10 July 2006 revised 1 September 2006 accepted 6 September 2006 doi 10.1111 j.1742-4658.2006.05492.x The dystroglycan adhesion complex consists of two noncovalently interacting proteins a-dystroglycan a peripheral extracellular subunit that is extensively glycosylated and the transmembrane b-dystroglycan whose cytosolic tail interacts with dystrophin thus linking the F-actin cytoskeleton to the extracellular matrix. Dystroglycan is thought to play a crucial role in the stability of the plasmalemma and forms strong contacts between the extracellular matrix and the cytoskeleton in a wide variety of tissues. Abnormal membrane targeting of dystroglycan subunits and or their aberrant post-translational modification are often associated with several pathologic conditions ranging from neuromuscular disorders to carcinomas. A putative functional hotspot of dystroglycan is represented by .
