A FAN1 point mutation associated with accelerated Huntington’s disease progression alters its PCNA-mediated assembly on DNA

Abstract FAN1 is an endo- and exo-nuclease involved in DNA and interstrand crosslink repair. Genome-wide association studies of people with Huntington’s disease revealed a strong association between the FAN1 R507H mutation and early disease onset, however the underlying mechanism(s) remains unclear....

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Main Authors: Jonas Aretz, Gayathri Jeyasankar, Anna Salerno-Kochan, Maren Thomsen, Gabriel Thieulin-Pardo, Tasir Haque, Edith Monteagudo, Dan Felsenfeld, Michael Finley, Thomas F. Vogt, Julien Boudet, Brinda C. Prasad
Format: Article
Language:English
Published: Nature Portfolio 2025-05-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-025-59324-x
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author Jonas Aretz
Gayathri Jeyasankar
Anna Salerno-Kochan
Maren Thomsen
Gabriel Thieulin-Pardo
Tasir Haque
Edith Monteagudo
Dan Felsenfeld
Michael Finley
Thomas F. Vogt
Julien Boudet
Brinda C. Prasad
author_facet Jonas Aretz
Gayathri Jeyasankar
Anna Salerno-Kochan
Maren Thomsen
Gabriel Thieulin-Pardo
Tasir Haque
Edith Monteagudo
Dan Felsenfeld
Michael Finley
Thomas F. Vogt
Julien Boudet
Brinda C. Prasad
author_sort Jonas Aretz
collection DOAJ
description Abstract FAN1 is an endo- and exo-nuclease involved in DNA and interstrand crosslink repair. Genome-wide association studies of people with Huntington’s disease revealed a strong association between the FAN1 R507H mutation and early disease onset, however the underlying mechanism(s) remains unclear. FAN1 has previously been implicated in modulating triplet repeat expansion in a PCNA dependent manner. To examine the role of PCNA on FAN1 activation, we solved the cryo-EM structures of a PCNA–FAN1–DNA complex. Our findings reveal that the FAN1 R507 residue directly interacts with PCNA D232. Biophysical interaction studies demonstrated that FAN1 enhances the binding affinity of PCNA for DNA, a synergistic effect disrupted in mutants carrying the R507H mutation. In contrast, PCNA does not affect the affinity of FAN1 for DNA but does modulate FAN1 activity upon ternary complex formation. The weakened and functionally altered FAN1 R507H–PCNA–DNA complex may partly impair the FAN1-mediated repair of CAG extrahelical extrusions, providing a potential explanation for the mutation’s role in accelerating disease progression.
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spelling doaj-art-89093fd6f5e74ae9aee2aa3174652e1d2025-08-20T02:25:16ZengNature PortfolioNature Communications2041-17232025-05-0116111410.1038/s41467-025-59324-xA FAN1 point mutation associated with accelerated Huntington’s disease progression alters its PCNA-mediated assembly on DNAJonas Aretz0Gayathri Jeyasankar1Anna Salerno-Kochan2Maren Thomsen3Gabriel Thieulin-Pardo4Tasir Haque5Edith Monteagudo6Dan Felsenfeld7Michael Finley8Thomas F. Vogt9Julien Boudet10Brinda C. Prasad11Proteros biostructures GmbHProteros biostructures GmbHProteros biostructures GmbHProteros biostructures GmbHProteros biostructures GmbHCHDI Management, Inc, the company that manages the scientific activities of CHDI Foundation, Inc.CHDI Management, Inc, the company that manages the scientific activities of CHDI Foundation, Inc.CHDI Management, Inc, the company that manages the scientific activities of CHDI Foundation, Inc.CHDI Management, Inc, the company that manages the scientific activities of CHDI Foundation, Inc.CHDI Management, Inc, the company that manages the scientific activities of CHDI Foundation, Inc.CHDI Management, Inc, the company that manages the scientific activities of CHDI Foundation, Inc.CHDI Management, Inc, the company that manages the scientific activities of CHDI Foundation, Inc.Abstract FAN1 is an endo- and exo-nuclease involved in DNA and interstrand crosslink repair. Genome-wide association studies of people with Huntington’s disease revealed a strong association between the FAN1 R507H mutation and early disease onset, however the underlying mechanism(s) remains unclear. FAN1 has previously been implicated in modulating triplet repeat expansion in a PCNA dependent manner. To examine the role of PCNA on FAN1 activation, we solved the cryo-EM structures of a PCNA–FAN1–DNA complex. Our findings reveal that the FAN1 R507 residue directly interacts with PCNA D232. Biophysical interaction studies demonstrated that FAN1 enhances the binding affinity of PCNA for DNA, a synergistic effect disrupted in mutants carrying the R507H mutation. In contrast, PCNA does not affect the affinity of FAN1 for DNA but does modulate FAN1 activity upon ternary complex formation. The weakened and functionally altered FAN1 R507H–PCNA–DNA complex may partly impair the FAN1-mediated repair of CAG extrahelical extrusions, providing a potential explanation for the mutation’s role in accelerating disease progression.https://doi.org/10.1038/s41467-025-59324-x
spellingShingle Jonas Aretz
Gayathri Jeyasankar
Anna Salerno-Kochan
Maren Thomsen
Gabriel Thieulin-Pardo
Tasir Haque
Edith Monteagudo
Dan Felsenfeld
Michael Finley
Thomas F. Vogt
Julien Boudet
Brinda C. Prasad
A FAN1 point mutation associated with accelerated Huntington’s disease progression alters its PCNA-mediated assembly on DNA
Nature Communications
title A FAN1 point mutation associated with accelerated Huntington’s disease progression alters its PCNA-mediated assembly on DNA
title_full A FAN1 point mutation associated with accelerated Huntington’s disease progression alters its PCNA-mediated assembly on DNA
title_fullStr A FAN1 point mutation associated with accelerated Huntington’s disease progression alters its PCNA-mediated assembly on DNA
title_full_unstemmed A FAN1 point mutation associated with accelerated Huntington’s disease progression alters its PCNA-mediated assembly on DNA
title_short A FAN1 point mutation associated with accelerated Huntington’s disease progression alters its PCNA-mediated assembly on DNA
title_sort fan1 point mutation associated with accelerated huntington s disease progression alters its pcna mediated assembly on dna
url https://doi.org/10.1038/s41467-025-59324-x
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