IngMarie Nilsson

IngMarie Nilsson


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Works at Department of Biochemistry and Biophysics
Visiting address Svante Arrhenius väg 16
Room A 425
Postal address Institutionen för biokemi och biofysik 106 91 Stockholm


Membrane proteins in health and disease.

N-linked glycosylation is the most frequent modification of secretory and membrane proteins in eukaryotic cells. Many human diseases are caused by inherited or acquired modifications in membrane proteins and several disorders are associated with deficiencies in the N-linked glycosylation pathway. Some diseases are caused by mutations that lead to a loss of function of the membrane protein expressed from the gene. Others arise when a specific protein undergoes a conformational rearrangement and/or aggregates.

At present, there are very few clues how mutations in genes of different membrane proteins cause such diverse disorders as cystic fibrosis, Alzheimer's diseases and lipodystrophy. To better understand and explain specific roles of membrane proteins involved in human diseases, work in our lab is focused on membrane protein topologies, using a glycosylation mapping approach. We have a special interest in problems related to the oligosaccharyl transferase complex that modifies proteins by glycosylation.


Group members

Åsa Tellgren-Roth, Researcher


Selected Publications

  • Cuviello F., Tellgren-Roth Å., Lara P., Ruud Selin F., Monné M., Bisaccia F., Nilsson I., and Ostuni A. (2015)
    Membrane insertion and topology of the amino-terminal domain TMD0 of multidrug-resistance associated protein 6 (MRP6).
    FEBS Letters, 589, 3921-8.
  • Sáenz A., Presto J., Lara P., Akinyi-Oloo L., Garcia-Fojeda B., Nilsson I., Johansson J., and Casals C. (2015)
    Folding and intramembraneous BRICHOS binding of the prosurfactant protein C transmembrane segment.
    J Biol. Chem., 290, 17628-41.
  • Lee H., Lara P., Ostuni A., Presto J., Johansson J., Nilsson I., and Kim H. A. (2014)
    Live-cell topology assessment of URG7, MRP6102 and SP-C using glycosylatable green fluorescent protein in mammalian cells.
    BBRC., 450, 1587-92.     
  • Wanngren J., Lara P., Öjemalm K., Maioli S., Moradi N., Chen L., Tjernberg L. O., Lundkvist J., Nilsson I., and Karlström H. (2014)
    Charged membrane integration and catalytic site conformation are two mechanisms behind the increased Ab42/Ab40 ratio by Presenilin familial Alzheimer-linked mutations.
    FEBS Open Bio., 4, 393-406.
  • Ostuni A., Lara, P., Armentano M.  F., Miglionico R., Salvia A. M., Mönnich M., Carmosino M., Lasorsa F. M., Monné M., Nilsson I.,and Bisaccia F. (2013)
    The hepatitis B x antigen anti-apoptotic URG7 is localized to the endoplasmic reticulum membrane.
    FEBS Letters, 587, 3058-62.
  • Hedin L., Öjemalm K., Bernsel A., Hennerdal A., Illergård A., Enquist K., Kauko A., Cristobal S., von Heijne G., Lerch-Bader M., Nilsson I. and Elofsson A. (2010)
    Membrane insertion of marginally hydrophobic transmembrane helices depends on sequence context.
    J. Mol. Biol., 396, 221-9.
  • Enquist K., Fransson M., Boekel C., Bengtsson I., Geiger K., Lang L., Pettersson A., Johansson S., von Heijne G. and Nilsson I. (2009)
    Membrane-integration characteristics of two ABC transporters, CFTR and P-glycoprotein.
    J. Mol. Biol., 387, 1153-64.
  • Lundin C., Johansson S., Johnson AE., Näslund J., von Heijne G. and Nilsson I. (2007)
    Stable insertion of Alzheimer Aβ peptide into the ER membrane strongly correlates with its length.
    FEBS Letters, 581, 3809-13.

Funding Sources

The group is supported by grants from the Swedish Cancer Foundation, the Swedish Foundation for Strategic Research, the Swedish Foundation for International Cooperation in Research and Higher Education (STINT), the Carl Tryggers Foundation, Stiftelsen för Gamla Tjänarinnor, Magnus Bergvalls Stiftelse (MBS), and from Henrik Granholms Stiftelse.

Last updated: June 17, 2020

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