TY - JOUR
T1 - Seipin
T2 - A mysterious protein
AU - Agarwal, Anil K.
AU - Garg, Abhimanyu
N1 - Funding Information:
The authors thank Robert I. Barnes for the mining of the GenBank database for homology to seipin and Jennifer Sprayberry for help with illustrations. The study was supported in part by the National Institutes of Health grants, R01-DK54387 and M01-RR00633, and by the Southwestern Medical Foundation.
PY - 2004/9
Y1 - 2004/9
N2 - In 2001, a locus for autosomal-recessive congenital generalized lipodystrophy was identified on chromosome 11q13 and mutations in a novel gene named Berardinelli-Seip congenital lipodystrophy 2 (BSCL2) were reported. Earlier this year, heterozygous mutations in the BSCL2 gene, restricted to the N-glycosylation (N-X-S/T) motif, were reported in autosomal-dominant distal hereditary motor neuropathy and Silver syndrome, which are disorders with distinctly different phenotypes from lipodystrophy. BSCL2 encodes seipin, a transmembrane protein that is localized to the endoplasmic reticulum. It is proposed that its homology to midasin, an AAA (ATPases associated with various cellular activities) domain-containing nuclear protein that is involved in RNA transport, might yield some clues as to how mutant forms of seipin cause two clinically distinct syndromes.
AB - In 2001, a locus for autosomal-recessive congenital generalized lipodystrophy was identified on chromosome 11q13 and mutations in a novel gene named Berardinelli-Seip congenital lipodystrophy 2 (BSCL2) were reported. Earlier this year, heterozygous mutations in the BSCL2 gene, restricted to the N-glycosylation (N-X-S/T) motif, were reported in autosomal-dominant distal hereditary motor neuropathy and Silver syndrome, which are disorders with distinctly different phenotypes from lipodystrophy. BSCL2 encodes seipin, a transmembrane protein that is localized to the endoplasmic reticulum. It is proposed that its homology to midasin, an AAA (ATPases associated with various cellular activities) domain-containing nuclear protein that is involved in RNA transport, might yield some clues as to how mutant forms of seipin cause two clinically distinct syndromes.
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U2 - 10.1016/j.molmed.2004.07.009
DO - 10.1016/j.molmed.2004.07.009
M3 - Article
C2 - 15350896
AN - SCOPUS:4444261794
SN - 1471-4914
VL - 10
SP - 440
EP - 444
JO - Trends in Molecular Medicine
JF - Trends in Molecular Medicine
IS - 9
ER -