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Gewählte Publikation:
SHR Neuro Krebs Kardio Lipid Stoffw Microb
Lundin, C; Nordström, R; Wagner, K; Windpassinger, C; Andersson, H; von Heijne, G; Nilsson, I.
Membrane topology of the human seipin protein.
FEBS Lett. 2006; 580(9):2281-2284
Doi: 10.1016/j.febslet.2006.03.040
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- Co-Autor*innen der Med Uni Graz
- Wagner Klaus
- Windpassinger Christian
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- Abstract:
- The Berardinelli-Seip congenital lipodystrophy type 2 (BSCL2) gene encodes an integral membrane protein, called seipin, of unknown function localized to the endoplasmic reticulum of eukaryotic cells. Seipin is associated with the heterogeneous genetic disease BSCL2, and mutations in an N-glycosylation motif links the protein to two other disorders, autosomal-dominant distal hereditary motor neuropathy type V and Silver syndrome. Here, we report a topological study of seipin using an in vitro topology mapping assay. Our results suggest that the predominant form of seipin is 462 residues long and has an N(cyt)-C(cyt) orientation with a long luminal loop between the two transmembrane helices.
- Find related publications in this database (using NLM MeSH Indexing)
- Amino Acid Motifs - genetics
- Chromosome Disorders - genetics
- Diabetes Mellitus, Lipoatrophic - genetics
- Endoplasmic Reticulum - genetics
- GTP-Binding Protein gamma Subunits - genetics
- Humans - genetics
- Intracellular Membranes - metabolism
- Protein Modification, Translational - genetics
- Protein Structure, Tertiary - genetics
- Find related publications in this database (Keywords)
- seipin
- N-linked glycosylation
- oligosaccharyl transferase
- topology mapping
- BCSL gene