Sodium hydrogen exchanger (NHE1) palmitoylation and potential functional regulation

Moriah J. Hovde, Danielle E. Bolland, Aryna Armand, Emily Pitsch, Clare Bakker, Amanda J. Kooiker, Joseph J. Provost, Roxanne A. Vaughan, Mark A. Wallert, James D. Foster

Research output: Contribution to journalArticlepeer-review

3 Scopus citations


Aims: Determine the effect of palmitoylation on the sodium hydrogen exchanger isoform 1 (NHE1), a member of the SLC9 family. Main methods: NHE1 expressed in native rat tissues or in heterologous cells was assessed for palmitoylation by acyl-biotinyl exchange (ABE) and metabolic labeling with [3H]palmitate. Cellular palmitoylation was inhibited using 2-bromopalmitate (2BP) followed by determination of NHE1 palmitoylation status, intracellular pH, stress fiber formation, and cell migration. In addition, NHE1 was activated with LPA treatment followed by determination of NHE1 palmitoylation status and LPA-induced change in intracellular pH was determined in the presence and absence of preincubation with 2BP. Key findings: In this study we demonstrate for the first time that NHE1 is palmitoylated in both cells and rat tissue, and that processes controlled by NHE1 including intracellular pH (pHi), stress fiber formation, and cell migration, are regulated in concert with NHE1 palmitoylation status. Importantly, LPA stimulates NHE1 palmitoylation, and 2BP pretreatment dampens LPA-induced increased pHi which is dependent on the presence of NHE1. Significance: Palmitoylation is a reversible lipid modification that regulates an array of critical protein functions including activity, trafficking, membrane microlocalization and protein-protein interactions. Our results suggest that palmitoylation of NHE1 and other control/signaling proteins play a major role in NHE1 regulation that could significantly impact multiple critical cellular functions.

Original languageEnglish (US)
Article number120142
JournalLife Sciences
StatePublished - Jan 1 2022
Externally publishedYes

Bibliographical note

Funding Information:
This work was supported by the University of North Dakota and grants ND EPSCoR Doctoral Dissertation Fellowship OIA-1355466 (MJH); P20 GM104360 (to UND) from the COBRE program and P20 GM103442 (to UND) from the INBRE program of the National Institute of General Medical Sciences . This work was also supported by Bemidji State University , the Lueken Family Foundation , and a Regenerative Medicine Minnesota Education Grant ( RMM-2017-EP-04 ) and University of San Diego Beckman Scholars Foundation.

Publisher Copyright:
© 2021 Elsevier Inc.


  • Acyl protein thioesterase
  • Cell migration
  • Intracellular pH
  • Palmitoyl acyl transferase
  • Post translational modification
  • Protein palmitoyl thioesterase
  • Stress fiber formation

PubMed: MeSH publication types

  • Journal Article


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