Academic Journal

Specificity of binding of the plectin actin-binding domain to beta4

التفاصيل البيبلوغرافية
العنوان: Specificity of binding of the plectin actin-binding domain to beta4
المؤلفون: Y H. M. Litjens, Jan Koster, Ingrid Kuikman, Ra Van Wilpe, José M. De Pereda, Arnoud Sonnenberg, Richard Hynes
المساهمون: The Pennsylvania State University CiteSeerX Archives
المصدر: http://www.molbiolcell.org/content/14/10/4039.full.pdf.
سنة النشر: 2003
المجموعة: CiteSeerX
الوصف: Plectin is a major component of the cytoskeleton and links the intermediate filament system to hemidesmosomes by binding to the integrin �4 subunit. Previously, a binding site for �4 was mapped on the actin-binding domain (ABD) of plectin and binding of �4 and F-actin to plectin was shown to be mutually exclusive. Here we show that only the ABDs of plectin and dystonin bind to �4, whereas those of other actin-binding proteins do not. Mutations of the ABD of plectin-1C show that Q131, R138, and N149 are critical for tight binding of the ABD to �4. These residues form a small cavity, occupied by a well-ordered water molecule in the crystal structure. The �4 binding pocket partly overlaps with the actin-binding sequence 2 (ABS2), previously shown to be essential for actin binding. Therefore, steric interference may render binding of �4 and F-actin to plectin mutually exclusive. Finally, we provide evidence indicating that the residues preceding the ABD in plectin-1A and-1C, although unable to mediate binding to �4 themselves, modulate the binding activity of the ABD for �4. These studies demonstrate the unique property of the plectin-ABD to bind to both F-actin and �4, and explain why several other ABD-containing proteins that are expressed in basal keratinocytes are not recruited into hemidesmosomes.
نوع الوثيقة: text
وصف الملف: application/pdf
اللغة: English
Relation: http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.325.2899; http://www.molbiolcell.org/content/14/10/4039.full.pdf
الاتاحة: http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.325.2899
http://www.molbiolcell.org/content/14/10/4039.full.pdf
Rights: Metadata may be used without restrictions as long as the oai identifier remains attached to it.
رقم الانضمام: edsbas.EA9DF541
قاعدة البيانات: BASE