COXFA4L2 upregulation preserves residual cytochrome c oxidase activity in COXFA4-related Leigh-like encephalopathy

M Micol Falabella S Sandra Lopez Calcerrada J Jana Aref J Jiaze Gao W William L. Macken C Chiara Pizzamiglio R Renata Kabiljo A Anna Lucia Francavilla P Pauline Gaignard A Antoine Pouzet J Jonathan Levy G Giulia Barcia J Jamie K. Leighton E Efstathia Chronopoulou G Germaine Pierre R Riza Köksal Özgül A Ali Dursun R Rebecca Halligan H Helen Mundy J Javeria Raza Alvi T Tipu Sultan W William James Craigen L Lisa Emrick J Jill A. Rosenfeld G Gehad Elmakkawy J Jihye Kim J Joseph J. Gleeson A Aboulfazl Rad G Gabriela Oprea M Maqbool Hussain K Khalil ur Rehman S Sadia Riaz R Robert W. Taylor (Mitochondrial Research Group, Translational and Clinical Research Institute, Faculty of Medical Sciences, Newcastle University, Newcastle upon Tyne, United Kingdom) V Vincent Procaccio M Maha S. Zaki E Erika Fernández-Vizarra C Ciro Leonardo Pierri M Michael G. Hanna H Henry Houlden R Reza Maroofian C Cristina Ugalde J Jan-Willem Taanman R Robert D. S. Pitceathly

Abstract

Abstract Primary mitochondrial diseases (PMDs) affect approximately 1 in 4300 individuals and cause early-onset neuromuscular and multisystem dysfunction with reduced lifespan. They result from pathogenic variants in mitochondrial or nuclear DNA that impair oxidative phosphorylation. Cytochrome c oxidase (COX; complex IV) deficiency is a well-established cause of PMD, leading to a broad spectrum of phenotypes. COXFA4 (cytochrome c oxidase subunit FA4), formerly NDUFA4, is a nuclear-encoded COX subunit, but its role in disease remains poorly defined. We report the largest genetically confirmed cohort of COXFA4-related PMD to date, comprising 13 individuals from 12 families with biallelic pathogenic COXFA4 variants. All present with Leigh-like encephalopathy and complete loss of COXFA4 protein; however, patient-derived fibroblasts retain residual COX activity, with upregulation of COXFA4L2 (cytochrome c oxidase subunit FA4-like 2), a poorly characterised paralog. Here, we show that COXFA4 is a late-stage COX assembly subunit and identify a paralog-mediated compensatory mechanism with translational potential.

Article Details

Volume / Issue Vol. 17, Issue 1
Published May 30, 2026
ISSN 2041-1723
Publisher Nature Portfolio

Journal Info

Nature Communications

Nature Portfolio

ISSN: 2041-1723 Open Access Life Sciences

Authors (43)

M

Micol Falabella

S

Sandra Lopez Calcerrada

J

Jana Aref

J

Jiaze Gao

W

William L. Macken

C

Chiara Pizzamiglio

R

Renata Kabiljo

A

Anna Lucia Francavilla

P

Pauline Gaignard

A

Antoine Pouzet

J

Jonathan Levy

G

Giulia Barcia

J

Jamie K. Leighton

E

Efstathia Chronopoulou

G

Germaine Pierre

R

Riza Köksal Özgül

A

Ali Dursun

R

Rebecca Halligan

H

Helen Mundy

J

Javeria Raza Alvi

T

Tipu Sultan

W

William James Craigen

L

Lisa Emrick

J

Jill A. Rosenfeld

G

Gehad Elmakkawy

J

Jihye Kim

J

Joseph J. Gleeson

A

Aboulfazl Rad

G

Gabriela Oprea

M

Maqbool Hussain

K

Khalil ur Rehman

S

Sadia Riaz

R

Robert W. Taylor

Mitochondrial Research Group, Translational and Clinical Research Institute, Faculty of Medical Sciences, Newcastle University, Newcastle upon Tyne, United Kingdom

V

Vincent Procaccio

M

Maha S. Zaki

E

Erika Fernández-Vizarra

C

Ciro Leonardo Pierri

M

Michael G. Hanna

H

Henry Houlden

R

Reza Maroofian

C

Cristina Ugalde

J

Jan-Willem Taanman

R

Robert D. S. Pitceathly