Differential binding of mutant (R116C) and wildtype alphaA crystallin to actin

Zachery Brown, Aldo Ponce, Kirsten Lampi, Lynn Hancock, Larry Takemoto

Research output: Contribution to journalArticlepeer-review

20 Scopus citations


Purpose: Quantitate the interaction of mutant (R116C) and wildtype human alphaA crystallins with actin. Methods: AlphaA crystallins, expressed in a recombinant system, were purified, followed by passage through an actin affinity column. Results: Binding of mutant alphaA crystallin was significantly less than binding of wildtype alphaA crystallin. Conclusions: The R116C mutation of alphaA crystallin found in human cataracts binds less to the cytoskeletal component actin. Since both alphaA crystallin and actin are necessary for proper development of the lens, decreased binding of the mutant protein to actin may perturb normal differentiation processes of lens cells which are necessary for transparency.

Original languageEnglish (US)
Pages (from-to)1051-1054
Number of pages4
JournalCurrent Eye Research
Issue number12
StatePublished - Dec 2007


  • AlphaA crystallin mutation
  • Human cataractogenesis

ASJC Scopus subject areas

  • Ophthalmology
  • Sensory Systems
  • Cellular and Molecular Neuroscience


Dive into the research topics of 'Differential binding of mutant (R116C) and wildtype alphaA crystallin to actin'. Together they form a unique fingerprint.

Cite this