Human α spectrin II and the Fanconi anemia proteins FANCA and FANCC interact to form a nuclear complex

Laura W. McMahon, Christopher E. Walsh, Muriel W. Lambert

Research output: Contribution to journalArticlepeer-review

77 Scopus citations


Fanconi anemia (FA) is a genetic disorder characterized by bone marrow failure, congenital abnormalities, cancer susceptibility, and a marked cellular hypersensitivity to DNA interstrand cross-linking agents, which correlates with a defect in ability to repair this type of damage. We have previously identified an approximately 230-kDa protein present in a nuclear protein complex in normal human lymphoblastoid cells that is involved in repair of DNA interstrand cross-links and shows reduced levels in FA-A cell nuclei. The FANCA gene appears to play a role in the stability or expression of this protein. We now show that p230 is a well known structural protein, human α spectrin II (αSpIIΣ*), and that levels of αSpIIΣ* are not only significantly reduced in FA-A cells but also in FA-B, FA-C and FA-D cells (i.e. in all FA cell lines tested), suggesting a role for these FA proteins in the stability or expression of αSpIIΣ*. These studies also show that αSpIIΣ* forms a complex in the nucleus with the FANCA and FANCC proteins, αSpIIΣ* may thus act as a scaffold to align or enhance interactions between FA proteins and proteins involved in DNA repair. These results suggest that FA represents a disorder in which there is a deficiency in αSpIIΣ*.

Original languageEnglish (US)
Pages (from-to)32904-32908
Number of pages5
JournalJournal of Biological Chemistry
Issue number46
StatePublished - Nov 12 1999

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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