title: Cyclophilins: proteins in search of function.
abstract: Cyclophilins constitute a subgroup of large family of proteins called immunophilins, which also include FKBPs and Parvulins. They are remarkably conserved in all genera, highlighting their pivotal role in important cellular processes. Most cyclophilins display PPIase enzymatic activity, multiplicity, diverse cellular locations and active role in protein folding which render them to be included in the class of diverse set of proteins called molecular chaperones. Due to their distinct PPIase function, besides protein disulfide isomerases and protein foldases, cyclophilins have been deemed necessary for in vivo chaperoning activity. Unlike other cellular chaperones, these proteins are specific in their respective targets. Not all cyclophilin proteins possess PPIase activity, indicating a loss of their PPIase activity during the course of evolution and gain of function independent of their PPIase activity. The PPIase function of cyclophilins is also compensated by their functional homologs, like FKBPs. Multiple cyclophilin members in plants like Arabidopsis and rice have been reported to be associated with diverse functions and regulatory pathways through their foldase, scaffolding, chaperoning or other unknown activities. Although many functions of plant cyclophilins were reported or suggested, the physiological relevance and molecular basis of stress-responsive expression of plant cyclophilins is still largely unknown. However, their wide distribution and ubiquitous nature signifies their fundamental importance in plant survival. Several of these members have also been directly linked to multiple stresses. This review attempts to deal with plant cyclophilins with respect to their role in stress response.
authors.affiliation: Sher-e-Kashmir University of Agricultural Sciences and Technology; Jammu, India.
authors.forename: Sumita
authors.initials: S
authors.lastname: Kumari
authors.affiliation: Stress Physiology and Molecular Biology Laboratory; School of Life Sciences; Jawaharlal Nehru University; New Delhi, India.
authors.forename: Suchismita
authors.initials: S
authors.lastname: Roy
authors.affiliation: Department of Biotechnology; Guru Nanak Dev University; Amritsar, India.
authors.forename: Prabhjeet
authors.initials: P
authors.lastname: Singh
authors.affiliation: Plant Molecular Biology; International Centre for Genetic Engineering and Biotechnology; New Delhi, India.
authors.forename: Sneh L
authors.initials: SL
authors.lastname: Singla-Pareek
authors.affiliation: Stress Physiology and Molecular Biology Laboratory; School of Life Sciences; Jawaharlal Nehru University; New Delhi, India.
authors.forename: Ashwani
authors.initials: A
authors.lastname: Pareek
mesh_terms: D000222:Adaptation, Physiological; D021983:Cyclophilins / Q000378:metabolism*; D019696:Peptidylprolyl Isomerase / Q000378:metabolism*; D010940:Plant Proteins / Q000378:metabolism*; D010944:Plants / Q000378:metabolism*; D013312:Stress, Physiological
chemical_list: D010940:Plant Proteins; D021983:Cyclophilins; D019696:Peptidylprolyl Isomerase
keywords: cyclophilin; protein folding; stress