Publications of Research Area B7
Characterization of the in vivo functions of
Signal-peptide-peptidase-like 2-a/b (SPPL2a/b) in mouse models
Teilprojektleiter: Paul Saftig
- The intramembrane protease SPPL2a promotes B cell development and controls endosomal traffic by cleavage of the invariant chain.Schneppenheim J, Dressel R, Hüttl S, Lüllmann-Rauch R, Engelke M, Dittmann K, Wienands J, Eskelinen EL, Hermans-Borgmeyer I, Fluhrer R, Saftig P, Schröder B. J Exp Med. 2013 Jan 14;210(1):41-58.
- Foamy Virus Envelope Protein Is a Substrate for Signal Peptide Peptidase-like 3 (SPPL3).Voss M, Fukumori A, Kuhn PH, Künzel U, Klier B, Grammer G, Haug-Kröper M, Kremmer E, Lichtenthaler SF, Steiner H, Schröder B, Haass C, Fluhrer R. J Biol Chem. 2012 Dec 21;287(52):43401-9.
- Signal-peptide-peptidase-like 2a (SPPL2a) is targeted to lysosomes/late endosomes by a tyrosine motif in its C-terminal tail. Behnke J, Schneppenheim J, Koch-Nolte F, Haag F, Saftig P, Schröder B. FEBS Lett. 2011 Oct 3;585(19):2951-7.
- Disrupted in renal carcinoma 2 (DIRC2), a novel transporter of the lysosomal membrane, is proteolytically processed by cathepsin L. Savalas LR, Gasnier B, Damme M, Lübke T, Wrocklage C, Debacker C, Jézégou A, Reinheckel T, Hasilik A, Saftig P, Schröder B. Biochem J. 2011 Oct 1;439(1):113-28.
- Two dileucine motifs mediate late endosomal/lysosomal targeting of transmembrane protein 192 (TMEM192) and a C-terminal cysteine residue is responsible for disulfide bond formation in TMEM192 homodimers. Behnke J, Eskelinen EL, Saftig P, Schröder B. Biochem J. 2011 Mar 1;434(2):219-31.
- Lysosomal membrane proteins: life between acid and neutral conditions. Saftig P, Schröder B, Blanz J. Biochem Soc Trans. 2010 Dec;38(6):1420-3
- The proteome of lysosomes. Schröder BA, Wrocklage C, Hasilik A, Saftig P. Proteomics. 2010 Nov;10(22):4053-76
- Molecular insights into mechanisms of intramembrane proteolysis through signal peptide peptidase (SPP). Schröder B, Saftig P. Biochem J. 2010 Apr 14;427(3):e1-3
