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Groupleader: Ingrid Haas

Function and Regulation of BiP 

Group Leader Ingrid Haas

Ingrid Haas

Function and Regulation of BiP

  • CV
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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 


2002 (work conducted at BZH)
BiP is feed-back regulated by control of protein translation efficiency.
Gülow K, Bienert D, Haas IG.
J Cell Sci. 2002 Jun 1;115(Pt 11):2443-52.

2000
Mannosidase action, independent of glucose trimming, is essential for proteasome-mediated degradation of unassembled glycosylated Ig light chains.
Chillarón J, Adán C, Haas IG.
Biol Chem. 2000 Dec;381(12):1155-64.

Homologs of the yeast Sec complex subunits Sec62p and Sec63p are abundant proteins in dog pancreas microsomes.
Tyedmers J, Lerner M, Bies C, Dudek J, Skowronek MH, Haas IG, Heim N, Nastainczyk W, Volkmer J, Zimmermann R.
Proc Natl Acad Sci U S A. 2000 Jun 20;97(13):7214-9.

Dissociation from BiP and retrotranslocation of unassembled immunoglobulin light chains are tightly coupled to proteasome activity.
Chillarón J, Haas IG.
Mol Biol Cell. 2000 Jan;11(1):217-26.

1999
Molecular characterization of a novel mammalian DnaJ-like Sec63p homolog.
Skowronek MH, Rotter M, Haas IG.
Biol Chem. 1999 Sep;380(9):1133-8.

Cycloheximide, a new tool to dissect specific steps in ER-associated degradation of different substrates.
Amshoff C, Jäck HM, Haas IG.
Biol Chem. 1999 Jun;380(6):669-77.

1998
The variable domain of nonassembled Ig light chains determines both their half-life and binding to the chaperone BiP.
Skowronek MH, Hendershot LM, Haas IG.
Proc Natl Acad Sci U S A. 1998 Feb 17;95(4):1574-8.

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.
Ermonval M, Cacan R, Gorgas K, Haas IG, Verbert A, Buttin G.
J Cell Sci. 1997 Feb;110 ( Pt 3):323-36

Assembly of immunoglobulin light chains as a prerequisite for secretion. A model for oligomerization-dependent subunit folding.
Leitzgen K, Knittler MR, Haas IG.
J Biol Chem. 1997 Jan 31;272(5):3117-23.

1995
Protein-mediated protein maturation in eukaryotes.
Haas IG.
FEBS Lett. 1995 Aug 1;369(1):72-5. Review.

Coordination of immunoglobulin chain folding and immunoglobulin chain assembly is essential for the formation of functional IgG.
Kaloff CR, Haas IG.
Immunity. 1995 Jun;2(6):629-37.

Roles of heavy and light chains in IgM polymerization.
Bornemann KD, Brewer JW, Beck-Engeser GB, Corley RB, Haas IG, Jäck HM.
Proc Natl Acad Sci U S A. 1995 May 23;92(11):4912-6.

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.
Knittler MR, Dirks S, Haas IG.
Proc Natl Acad Sci U S A. 1995 Feb 28;92(5):1764-8.

1994
8 groups of scientists from 7 European countries sharing scientific interest in Cells as Protein Factories (Meeting Title) decided to have yearly meetings with the First being organized in Heidelberg (Germany).  Group Leaders involved were: Ineke Braakman (The Netherlands), Myriam Ermonval (France), Ingrid Haas (Germany), Aldo Ceriotti, Rorto Sitia,  (Italy) Erwin Ivessa (Austria), Neil Bulleid (Great Britain), Marja Makarow (Finland). Invired Guests in Heidelberg were: Ulrich Hartl (Munich) and Stefan Jentsch (Munich). The following meetings were to take place in Paris (France), and Belgirate (Italy).
BiP (GRP78), an essential hsp70 resident protein in the endoplasmic reticulum.
Haas IG.
Experientia. 1994 Nov 30;50(11-12):1012-20. Review.

1993
Expression of highly active sex-inducing pheromone of Volvox carteri f. nagariensis in a mammalian cell system.
Jaenicke L, Feldwisch O, Merkl B, Cremer A, Haas IG.
FEBS Lett. 1993 Feb 1;316(3):257-60.

1992
Interaction of BiP with newly synthesized immunoglobulin light chain molecules: cycles of sequential binding and release.
Knittler MR, Haas IG.
EMBO J. 1992 Apr;11(4):1573-81.

The gene coding for the immunoglobulin heavy chain binding protein BiP (Hsce-70) maps to mouse chromosome 2.
Haas IG, Simon-Chazottes D, Guénet JL.
Mamm Genome. 1992;3(11):659-60.

1991
BiP--a heat shock protein involved in immunoglobulin chain assembly.
Haas IG.
Curr Top Microbiol Immunol. 1991;167:71-82. Review.

1988
cDNA cloning of the immunoglobulin heavy chain binding protein.
Haas IG, Meo T.
Proc Natl Acad Sci U S A. 1988 Apr;85(7):2250-4.

1984
Immunoglobulin heavy chain toxicity in plasma cells is neutralized by fusion to pre-B cells.
Haas IG, Wabl MR.
Proc Natl Acad Sci U S A. 1984 Nov;81(22):7185-8.

1983
Immunoglobulin heavy chain binding protein.
Haas IG, Wabl M.
Nature. 1983 Nov 24-30;306(5941):387-9.

1980
Simultaneous expression of mouse immunoglobulins M and D is determined by the same homolog of chromosome 12.
Wabl MR, Johnson JP, Haas IG, Tenkhoff M, Meo T, Inan R.
Proc Natl Acad Sci U S A. 1980 Nov;77(11):6793-6.

Effect of the aggregational state on the mitogenicity of lipoprotein from the outer membrane of Escherichia coli.
Haas IG, Simon E, Bessler WG.
Immunobiology. 1980 Jan;156(4-5):418-28.

Contact



Heidelberg University
Biochemistry Center (BZH)
Im Neuenheimer Feld 328
69120 Heidelberg

E-Mail:
IG.Haas@t-online.de


LOGO Biochemizentrum Heidelberg Heidelberg University Biochemistry Center (BZH)
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