title: Multidimensional significance of crystallin protein-protein interactions and their implications in various human diseases.
abstract: BACKGROUND
  Crystallins are the important structural and functional proteins in the eye lens responsible for refractive index. Post-translational modifications (PTMs) and mutations are major causative factors that affect crystallin structural conformation and functional characteristics thus playing a vital role in the etiology of cataractogenesis.
  
  
  METHODS
  The significance of crystallin protein-protein interactions (PPIs) in the lens and non-lenticular tissues is summarized.
  
  
  CONCLUSIONS
  Aberrancy of PPIs between crystallin, its associated protein and metal ions has been accomplished in various human diseases including cataract. A detailed account on multidimensional structural and functional significance of crystallin PPI in humans must be brought into limelight, in order to understand the biochemical and molecular basis augmenting the aberrancies of such interaction. In this scenario, the present review is focused to shed light on studies which will aid to expand our present understanding on disease pathogenesis related to loss of PPI thereby paving the way for putative future therapeutic targets to curb such diseases.
  
  
  CONCLUSIONS
  The interactions with α-crystallins always aid to protect their structural and functional characteristics. The up-regulation of αB-crystallin in the non-lenticular tissues always decodes as biomarker for various stress related disorders. For better understanding and treatment of various diseases, PPI studies provide overall outline about the structural and functional characteristics of the proteins. This information not only helps to find out the route of cataractogenesis but also aid to identify potential molecules to inhibit/prevent the further development of such complicated phenomenon. This article is part of a Special Issue entitled Crystallin Biochemistry in Health and Disease.
authors.affiliation: Department of Marine Biotechnology, Bharathidasan University, Tiruchirapalli 620024, Tamil Nadu, India. Electronic address: anbumbt@bdu.ac.in.
authors.forename: Kumarasamy
authors.initials: K
authors.lastname: Anbarasu
authors.affiliation: Department of Marine Biotechnology, Bharathidasan University, Tiruchirapalli 620024, Tamil Nadu, India.
authors.forename: Jeyarajan
authors.initials: J
authors.lastname: Sivakumar
mesh_terms: D001665:Binding Sites; D009202:Cardiomyopathies / Q000378:metabolism*; D002386:Cataract / Q000378:metabolism*; D003459:Crystallins / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D009369:Neoplasms / Q000378:metabolism*; D019636:Neurodegenerative Diseases / Q000378:metabolism*; D011485:Protein Binding; D025941:Protein Interaction Mapping
chemical_list: D003459:Crystallins
keywords: Cataract; Crystallin; Mutation; Protein–protein interaction