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Investigation of Calcineurin B Homologous Protein (CHP) Isoform Specific Function

Mammalian cells ubiquitously express the Sodium‐Hydrogen Exchanger Isoform 1 (NHE1) a membrane transporter responsible for intracellular pHi, motility and proliferation. Calcineurin B Homologous Protein (CHP) in part regulates activation and kinetics of the NHE1. CHP has two isoforms, CHP1 and CHP2, whose physiological function remains unclear but both have a unique role in nascent tumor survival. CHP binds NHE via the N and C terminal domains. There is a considerable tertiary structure between both the N terminal domains (amino acids 1–90) and the C terminal domain (aa 111/110–195/196) with a 72% and 74% conserved homology, an intervening loop domain is unique to each CUR. This signature domain CHP unique region (CUR: CHP1 R91 to S110 and CHP2 R91 to S111) when bound to NHE has a specific and distinct structure indicating its potential role in effecting CHP‐NHE1 related functions. The purpose of this study is to investigate how the these CHP unique regions contribute to CHP isoform cell function, specifically cell proliferation and location. Using site directed mutagenesis, we have generated epitope tagged (DDK and MYC) wild type versions of both isoforms of CHP and a variant with the respective CUR domain deleted (CHP1 ΔCUR1 and CHP2ΔCUR2). To distinguish the importance of the CUR domains we have swapped CUR domains between each CHP (CHP2(CUR1) and CHP1(CUR2). These mutations will be expressed in lung fibroblasts expressing NHE1 (CCL39) and PS120 cells (null NHE1 expressing CCL39 derivatives) to determine the impact of each CUR domain on cellular location in the absence and presence of NHE1 and on cell proliferation. We hypothesize that the CUR domain is critical for CHP isoform specific function and NHE1 interactions and present the role of both CHP isoforms on NHE1 related behavior.