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The sHSP and molecular chaperone, aB crystallin, regulates microtubule assembly
Author(s) -
Clark John I,
Houck Scott A.,
Ghosh Joy G.
Publication year - 2008
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.22.1_supplement.1006.1
Subject(s) - microtubule , tubulin , protein subunit , microbiology and biotechnology , chaperone (clinical) , chemistry , biophysics , biology , biochemistry , gene , medicine , pathology
Purpose: The small heat‐shock protein (sHSP) αB crystallin, which protects against unfolding and aggregation of proteins has a regulatory effect on microtubule assembly. The sequences responsible for αB crystallin ‐ microtubule interactions were identified and tested. Methods: Five interactive sequences in αB crystallin were identified and studied for their effects on the assembly of microtubules using synthetic peptides and mutants of αB crystallin. Assembly of microtubules was measured using a fluorescence DAPI assay (PloS one 6:3498). Results: αB crystallin inhibited microtubule assembly at molar ratios >2:1 αB crystallin:tubulin and promoted microtubule assembly at molar ratios between 1:4 – 2:1. The synthetic peptide corresponding to the αB crystallin interactive sequence, 113 FISREFHR 120 , partially inhibited microtubule assembly. In contrast, the peptides 131 LTITSSLSSDGV 142 and 156 ERTIPITRE 164 promoted microtubule assembly. Mutations in these sequences altered the nature of the interactions with microtubules. Conclusion: Three interactive sequences on the surface of human αB crystallin modulate microtubule assembly through the dynamic subunit model of small heat shock proteins.