ICMT supports BRAF <sup>V600E</sup> -driven tumor growth by membrane targeting of the CAAX protein INPP5E

X Xijie Yang (Department of Medicine, Huddinge, Karolinska Institutet) X Xi Qiao (Department of Medicine, Huddinge, Karolinska Institutet) S Sarah Schmidt (Department of Medicine, Huddinge, Karolinska Institutet) E Ella A. Eklund C Carolina Ebner-Walter (Department of Medicine, Huddinge, Karolinska Institutet) E Emil Ivarsson (Sahlgrenska Center for Cancer Research, University of Gothenburg) M Michelle Ann Crespo (Department of Medicine, Huddinge, Karolinska Institutet) N Nadieh Kersemakers (Department of Medicine, Huddinge, Karolinska Institutet) J Jozefina J. Dzanan B Bjarni Thorisson (Sahlgrenska Center for Cancer Research, University of Gothenburg) C Christine Lundgren (Sahlgrenska Center for Cancer Research, University of Gothenburg) H Hooi Ching Lim (Sahlgrenska Center for Cancer Research, University of Gothenburg) S Sam Shkoukani (Sahlgrenska Center for Cancer Research, University of Gothenburg) E Elin Tüksammel (Department of Medicine, Huddinge, Karolinska Institutet) X Xiufeng Xu (Department of Medicine, Huddinge, Karolinska Institutet) V Volkan I. Sayin M Mar Martín-Fontecha (Organic Chemistry Department, Faculty of Optics and Optometry, Universidad Complutense de Madrid) S Silvia Ortega-Gutiérrez (Department of Organic Chemistry) M Martin Dalin (Sahlgrenska Center for Cancer Research, University of Gothenburg) M Martin O. Bergo (Department of Medicine, Karolinska Institutet)

Abstract

Isoprenylcysteine carboxyl methyltransferase (ICMT) catalyzes C-terminal methylation of prenylated CAAX proteins, a final processing step promoting membrane association and signaling. Although ICMT has been pursued to disrupt RAS membrane targeting, its role in BRAF V600E -driven cancers and critical substrates remains unclear. Here, genetic and pharmacologic (UCM-1336) ICMT inhibition suppressed proliferation and invasion in BRAF V600E -mutant melanoma cells and reduced tumor growth in xenografts and mice. ICMT knockdown inhibited proliferation of BRAF-inhibitor-resistant melanoma cells. We identify INPP5E as an ICMT-dependent substrate: ICMT inhibition reduced INPP5E methylation, displaced it from membranes, and increased PI(4,5)P 2 . Forced INPP5E membrane targeting partially rescued growth defects caused by ICMT inhibition. These findings implicate an ICMT-INPP5E-axis that supports BRAF V600E -driven tumor growth.

Article Details

Volume / Issue Vol. 123, Issue 20
Published May 19, 2026
ISSN 0027-8424
Publisher National Academy of Sciences

Authors (20)

X

Xijie Yang

Department of Medicine, Huddinge, Karolinska Institutet

X

Xi Qiao

Department of Medicine, Huddinge, Karolinska Institutet

S

Sarah Schmidt

Department of Medicine, Huddinge, Karolinska Institutet

E

Ella A. Eklund

C

Carolina Ebner-Walter

Department of Medicine, Huddinge, Karolinska Institutet

E

Emil Ivarsson

Sahlgrenska Center for Cancer Research, University of Gothenburg

M

Michelle Ann Crespo

Department of Medicine, Huddinge, Karolinska Institutet

N

Nadieh Kersemakers

Department of Medicine, Huddinge, Karolinska Institutet

J

Jozefina J. Dzanan

B

Bjarni Thorisson

Sahlgrenska Center for Cancer Research, University of Gothenburg

C

Christine Lundgren

Sahlgrenska Center for Cancer Research, University of Gothenburg

H

Hooi Ching Lim

Sahlgrenska Center for Cancer Research, University of Gothenburg

S

Sam Shkoukani

Sahlgrenska Center for Cancer Research, University of Gothenburg

E

Elin Tüksammel

Department of Medicine, Huddinge, Karolinska Institutet

X

Xiufeng Xu

Department of Medicine, Huddinge, Karolinska Institutet

V

Volkan I. Sayin

M

Mar Martín-Fontecha

Organic Chemistry Department, Faculty of Optics and Optometry, Universidad Complutense de Madrid

S

Silvia Ortega-Gutiérrez

Department of Organic Chemistry

M

Martin Dalin

Sahlgrenska Center for Cancer Research, University of Gothenburg

M

Martin O. Bergo

Department of Medicine, Karolinska Institutet