TY - JOUR
T1 - Regulation of the Fanconi Anemia Group C Protein through Proteolytic Modification
AU - Brodeur, Isabelle
AU - Goulet, Isabelle
AU - Tremblay, Cédric S.
AU - Charbonneau, Chantal
AU - Delisle, Marie Chantal
AU - Godin, Chantal
AU - Huard, Caroline
AU - Khandjian, Edward W.
AU - Buchwald, Manuel
AU - Lévesque, Georges
AU - Carreau, Madeleine
PY - 2004/2/6
Y1 - 2004/2/6
N2 - The function of the Fanconi anemia group C protein (FANCC) is still unknown, though many studies point to a role in damage response signaling. Unlike other known FA proteins, FANCC is mainly localized to the cytoplasm and is thought to act as a messenger of cellular damage rather than an effector of repair. FANCC has been shown to interact with several cytoplasmic and nuclear proteins and to delay the onset of apoptosis through redox regulation of GSTP1. We investigated the fate and function of FANCC during apoptosis. Here we show that FANCC undergoes proteolytic modification by a caspase into a predominant 47-kDa ubiquitinated protein fragment. Lack of proteolytic modification at the putative cleavage site delays apoptosis but does not affect MMC complementation. These results suggest that FANCC function is regulated through proteolytic processing.
AB - The function of the Fanconi anemia group C protein (FANCC) is still unknown, though many studies point to a role in damage response signaling. Unlike other known FA proteins, FANCC is mainly localized to the cytoplasm and is thought to act as a messenger of cellular damage rather than an effector of repair. FANCC has been shown to interact with several cytoplasmic and nuclear proteins and to delay the onset of apoptosis through redox regulation of GSTP1. We investigated the fate and function of FANCC during apoptosis. Here we show that FANCC undergoes proteolytic modification by a caspase into a predominant 47-kDa ubiquitinated protein fragment. Lack of proteolytic modification at the putative cleavage site delays apoptosis but does not affect MMC complementation. These results suggest that FANCC function is regulated through proteolytic processing.
UR - http://www.scopus.com/inward/record.url?scp=10744224928&partnerID=8YFLogxK
U2 - 10.1074/jbc.M301291200
DO - 10.1074/jbc.M301291200
M3 - Article
C2 - 14625294
AN - SCOPUS:10744224928
SN - 0021-9258
VL - 279
SP - 4713
EP - 4720
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 6
ER -