RESEARCH GROUPS
PAGES
Groupleader: Ingrid Haas
Ingrid Haas
Function and Regulation of BiP
select submenu
CV
Academic Training and Positions
|
1977-1979 |
PhD in the Department of V. Braun, Institute for Microbiology, University of Tübingen, Germany |
|
1979-1984 |
Postdoctoral and Max Planck Fellow with M. Wabl at the Friedrich-Miescher Laboratory of the Max-Planck Society, Tübingen, Germany Discovery of BiP |
|
1984-1987 |
EMBO Fellow with A, Coutinho and Fellow of the Fondation pour la Recherche Médicale with T. Meo at the Pasteur-Institute in Paris, France Molecular Cloning of BiP |
|
1987-1993 |
Group Leader in the Department of K. Rajewsky at the Genetics Institute, University of Cologne, Germany Interaction of BiP with Immunoglobulin chains |
|
1992 |
Habilitation in Genetics and venia legendi in the Faculty of Mathematical and Natural Sciences, University of Cologne, Germany |
|
1993-2001 |
Group Leader at the Biochemie-Zentrum, University of Heidelberg (BZH), Germany Function and Regulation of BiP |
|
1993-1998 |
Heisenberg Fellow at the BZH |
|
1998-2001 |
DFG-Group Leader Position at the BZH |
|
1.5.2001 |
Group Leader in the Department of R. Kemler, Director of Molecular Embryology, at the Max Planck Institute for Immunology and Epigenetics in Freiburg, Germany |
Publications
BiP is feed-back regulated by control of protein translation efficiency. J Cell Sci. 115(Pt 11):2443-52.
Gülow K, Bienert D, Haas IG. (2002)
Dissociation from BiP and retrotranslocation of unassembled immunoglobulin light chains are tightly coupled to proteasome activity. Mol Biol Cell. 11(1):217-26.
Chillarón J, Haas IG. (2000)
Homologs of the yeast Sec complex subunits Sec62p and Sec63p are abundant proteins in dog pancreas microsomes. Proc Natl Acad Sci U S A. 97(13):7214-9.
Tyedmers J, Lerner M, Bies C, Dudek J, Skowronek MH, Haas IG, Heim N, Nastainczyk W, Volkmer J, Zimmermann R. (2000)
Mannosidase action, independent of glucose trimming, is essential for proteasome-mediated degradation of unassembled glycosylated Ig light chains. Biol Chem. 381(12):1155-64.
Chillarón J, Adán C, Haas IG. (2000)
Cycloheximide, a new tool to dissect specific steps in ER-associated degradation of different substrates. Biol Chem. 380(6):669-77.
Amshoff C, Jäck HM, Haas IG. (1999)
Molecular characterization of a novel mammalian DnaJ-like Sec63p homolog. Biol Chem. 380(9):1133-8.
Skowronek MH, Rotter M, Haas IG. (1999)
The variable domain of nonassembled Ig light chains determines both their half-life and binding to the chaperone BiP. Proc Natl Acad Sci U S A. 95(4):1574-8.
Skowronek MH, Hendershot LM, Haas IG. (1998)
Assembly of immunoglobulin light chains as a prerequisite for secretion. A model for oligomerization-dependent subunit folding. J Biol Chem. 272(5):3117-23.
Leitzgen K, Knittler MR, Haas IG. (1997)
Differential fate of glycoproteins carrying a monoglucosylated form of truncated N-glycan in a new CHO line, MadIA214214, selected for a thermosensitive secretory defect. J Cell Sci. 110 ( Pt 3):323-36
Ermonval M, Cacan R, Gorgas K, Haas IG, Verbert A, Buttin G. (1997)
Coordination of immunoglobulin chain folding and immunoglobulin chain assembly is essential for the formation of functional IgG. Immunity. 2(6):629-37.
Kaloff CR, Haas IG. (1995)
Molecular chaperones involved in protein degradation in the endoplasmic reticulum: quantitative interaction of the heat shock cognate protein BiP with partially folded immunoglobulin light chains that are degraded in the endoplasmic reticulum. Proc Natl Acad Sci U S A. 92(5):1764-8.
Knittler MR, Dirks S, Haas IG. (1995)
Protein-mediated protein maturation in eukaryotes. FEBS Lett. 369(1):72-5. Review.
Haas IG. (1995)
Roles of heavy and light chains in IgM polymerization. Proc Natl Acad Sci U S A. 92(11):4912-6.
Bornemann KD, Brewer JW, Beck-Engeser GB, Corley RB, Haas IG, Jäck HM. (1995)
BiP (GRP78), an essential hsp70 resident protein in the endoplasmic reticulum. Experientia. 50(11-12):1012-20. Review.
Haas IG. (1994)
Expression of highly active sex-inducing pheromone of Volvox carteri f. nagariensis in a mammalian cell system. FEBS Lett. 316(3):257-60.
Jaenicke L, Feldwisch O, Merkl B, Cremer A, Haas IG. (1993)
Interaction of BiP with newly synthesized immunoglobulin light chain molecules: cycles of sequential binding and release. EMBO J. 11(4):1573-81.
Knittler MR, Haas IG. (1992)
The gene coding for the immunoglobulin heavy chain binding protein BiP (Hsce-70) maps to mouse chromosome 2. Mamm Genome. 3(11):659-60.
Haas IG, Simon-Chazottes D, Guénet JL. (1992)
BiP--a heat shock protein involved in immunoglobulin chain assembly. Curr Top Microbiol Immunol. 167:71-82. Review.
Haas IG. (1991)
cDNA cloning of the immunoglobulin heavy chain binding protein. Proc Natl Acad Sci U S A. 85(7):2250-4.
Haas IG, Meo T. (1988)
Immunoglobulin heavy chain toxicity in plasma cells is neutralized by fusion to pre-B cells. Proc Natl Acad Sci U S A. 81(22):7185-8.
Haas IG, Wabl MR. (1984)
Immunoglobulin heavy chain binding protein. Nature 24-30;306(5941):387-9.
Haas IG, Wabl M. (1983)
Effect of the aggregational state on the mitogenicity of lipoprotein from the outer membrane of Escherichia coli. Immunobiology. 156(4-5):418-28.
Haas IG, Simon E, Bessler WG. (1980)
Simultaneous expression of mouse immunoglobulins M and D is determined by the same homolog of chromosome 12. Proc Natl Acad Sci U S A. 77(11):6793-6.
Wabl MR, Johnson JP, Haas IG, Tenkhoff M, Meo T, Inan R. (1980)
Gülow K, Bienert D, Haas IG. (2002)
Dissociation from BiP and retrotranslocation of unassembled immunoglobulin light chains are tightly coupled to proteasome activity. Mol Biol Cell. 11(1):217-26.
Chillarón J, Haas IG. (2000)
Homologs of the yeast Sec complex subunits Sec62p and Sec63p are abundant proteins in dog pancreas microsomes. Proc Natl Acad Sci U S A. 97(13):7214-9.
Tyedmers J, Lerner M, Bies C, Dudek J, Skowronek MH, Haas IG, Heim N, Nastainczyk W, Volkmer J, Zimmermann R. (2000)
Mannosidase action, independent of glucose trimming, is essential for proteasome-mediated degradation of unassembled glycosylated Ig light chains. Biol Chem. 381(12):1155-64.
Chillarón J, Adán C, Haas IG. (2000)
Cycloheximide, a new tool to dissect specific steps in ER-associated degradation of different substrates. Biol Chem. 380(6):669-77.
Amshoff C, Jäck HM, Haas IG. (1999)
Molecular characterization of a novel mammalian DnaJ-like Sec63p homolog. Biol Chem. 380(9):1133-8.
Skowronek MH, Rotter M, Haas IG. (1999)
The variable domain of nonassembled Ig light chains determines both their half-life and binding to the chaperone BiP. Proc Natl Acad Sci U S A. 95(4):1574-8.
Skowronek MH, Hendershot LM, Haas IG. (1998)
Assembly of immunoglobulin light chains as a prerequisite for secretion. A model for oligomerization-dependent subunit folding. J Biol Chem. 272(5):3117-23.
Leitzgen K, Knittler MR, Haas IG. (1997)
Differential fate of glycoproteins carrying a monoglucosylated form of truncated N-glycan in a new CHO line, MadIA214214, selected for a thermosensitive secretory defect. J Cell Sci. 110 ( Pt 3):323-36
Ermonval M, Cacan R, Gorgas K, Haas IG, Verbert A, Buttin G. (1997)
Coordination of immunoglobulin chain folding and immunoglobulin chain assembly is essential for the formation of functional IgG. Immunity. 2(6):629-37.
Kaloff CR, Haas IG. (1995)
Molecular chaperones involved in protein degradation in the endoplasmic reticulum: quantitative interaction of the heat shock cognate protein BiP with partially folded immunoglobulin light chains that are degraded in the endoplasmic reticulum. Proc Natl Acad Sci U S A. 92(5):1764-8.
Knittler MR, Dirks S, Haas IG. (1995)
Protein-mediated protein maturation in eukaryotes. FEBS Lett. 369(1):72-5. Review.
Haas IG. (1995)
Roles of heavy and light chains in IgM polymerization. Proc Natl Acad Sci U S A. 92(11):4912-6.
Bornemann KD, Brewer JW, Beck-Engeser GB, Corley RB, Haas IG, Jäck HM. (1995)
BiP (GRP78), an essential hsp70 resident protein in the endoplasmic reticulum. Experientia. 50(11-12):1012-20. Review.
Haas IG. (1994)
Expression of highly active sex-inducing pheromone of Volvox carteri f. nagariensis in a mammalian cell system. FEBS Lett. 316(3):257-60.
Jaenicke L, Feldwisch O, Merkl B, Cremer A, Haas IG. (1993)
Interaction of BiP with newly synthesized immunoglobulin light chain molecules: cycles of sequential binding and release. EMBO J. 11(4):1573-81.
Knittler MR, Haas IG. (1992)
The gene coding for the immunoglobulin heavy chain binding protein BiP (Hsce-70) maps to mouse chromosome 2. Mamm Genome. 3(11):659-60.
Haas IG, Simon-Chazottes D, Guénet JL. (1992)
BiP--a heat shock protein involved in immunoglobulin chain assembly. Curr Top Microbiol Immunol. 167:71-82. Review.
Haas IG. (1991)
cDNA cloning of the immunoglobulin heavy chain binding protein. Proc Natl Acad Sci U S A. 85(7):2250-4.
Haas IG, Meo T. (1988)
Immunoglobulin heavy chain toxicity in plasma cells is neutralized by fusion to pre-B cells. Proc Natl Acad Sci U S A. 81(22):7185-8.
Haas IG, Wabl MR. (1984)
Immunoglobulin heavy chain binding protein. Nature 24-30;306(5941):387-9.
Haas IG, Wabl M. (1983)
Effect of the aggregational state on the mitogenicity of lipoprotein from the outer membrane of Escherichia coli. Immunobiology. 156(4-5):418-28.
Haas IG, Simon E, Bessler WG. (1980)
Simultaneous expression of mouse immunoglobulins M and D is determined by the same homolog of chromosome 12. Proc Natl Acad Sci U S A. 77(11):6793-6.
Wabl MR, Johnson JP, Haas IG, Tenkhoff M, Meo T, Inan R. (1980)
Contact
Heidelberg University
Biochemistry Center (BZH)
Im Neuenheimer Feld 328
69120 Heidelberg
Biochemistry Center (BZH)
Im Neuenheimer Feld 328
69120 Heidelberg
E-Mail:
IG.Haas@t-online.de