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.