The carboxyl terminus of fance recruits FANCD2 to the fanconi anemia (FA) E3 ligase complex to promote the FA DNA repair pathway

David Polito; Scott Cukras; Xiaozhe Wang; Paige Spence; Lisa Moreau; Alan D. D'Andrea; Younghoon Kee

doi:10.1074/jbc.M113.533976

The carboxyl terminus of fance recruits FANCD2 to the fanconi anemia (FA) E3 ligase complex to promote the FA DNA repair pathway

David Polito, Scott Cukras, Xiaozhe Wang, Paige Spence, Lisa Moreau, Alan D. D'Andrea, Younghoon Kee

Department of New Biology

Research output: Contribution to journal › Article › peer-review

25 Scopus citations

Abstract

Background: Monoubiquitination of FANCD2 and FANCI is critical in the FA pathway. Results: Specific mutations in FANCE that disrupt FANCD2 binding impair the FA pathway. Conclusion: Inhibition of the FANCE-FANCD2 interaction via FANCE point mutations in the C terminus disrupts the FA pathway. Significance: Recruitment of FANCD2 and FANCI to the FA E3 ligase is a critical step in the FA pathway.

Original language	English
Pages (from-to)	7003-7010
Number of pages	8
Journal	Journal of Biological Chemistry
Volume	289
Issue number	10
DOIs	https://doi.org/10.1074/jbc.M113.533976
State	Published - 7 Mar 2014

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title = "The carboxyl terminus of fance recruits FANCD2 to the fanconi anemia (FA) E3 ligase complex to promote the FA DNA repair pathway",

abstract = "Background: Monoubiquitination of FANCD2 and FANCI is critical in the FA pathway. Results: Specific mutations in FANCE that disrupt FANCD2 binding impair the FA pathway. Conclusion: Inhibition of the FANCE-FANCD2 interaction via FANCE point mutations in the C terminus disrupts the FA pathway. Significance: Recruitment of FANCD2 and FANCI to the FA E3 ligase is a critical step in the FA pathway.",

author = "David Polito and Scott Cukras and Xiaozhe Wang and Paige Spence and Lisa Moreau and D'Andrea, \{Alan D.\} and Younghoon Kee",

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T1 - The carboxyl terminus of fance recruits FANCD2 to the fanconi anemia (FA) E3 ligase complex to promote the FA DNA repair pathway

AU - Polito, David

AU - Cukras, Scott

AU - Wang, Xiaozhe

AU - Spence, Paige

AU - Moreau, Lisa

AU - D'Andrea, Alan D.

AU - Kee, Younghoon

PY - 2014/3/7

Y1 - 2014/3/7

N2 - Background: Monoubiquitination of FANCD2 and FANCI is critical in the FA pathway. Results: Specific mutations in FANCE that disrupt FANCD2 binding impair the FA pathway. Conclusion: Inhibition of the FANCE-FANCD2 interaction via FANCE point mutations in the C terminus disrupts the FA pathway. Significance: Recruitment of FANCD2 and FANCI to the FA E3 ligase is a critical step in the FA pathway.

AB - Background: Monoubiquitination of FANCD2 and FANCI is critical in the FA pathway. Results: Specific mutations in FANCE that disrupt FANCD2 binding impair the FA pathway. Conclusion: Inhibition of the FANCE-FANCD2 interaction via FANCE point mutations in the C terminus disrupts the FA pathway. Significance: Recruitment of FANCD2 and FANCI to the FA E3 ligase is a critical step in the FA pathway.

UR - https://www.scopus.com/pages/publications/84896786442

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DO - 10.1074/jbc.M113.533976

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JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 10

ER -

The carboxyl terminus of fance recruits FANCD2 to the fanconi anemia (FA) E3 ligase complex to promote the FA DNA repair pathway

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