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Stable insertion of Alzheimer Aβ peptide into the ER membrane strongly correlates with its length
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för biokemi och biofysik.
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för biokemi och biofysik.
Vise andre og tillknytning
2007 (engelsk)Inngår i: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 581, nr 20, s. 3809-3813Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Alzheimer's disease is characterized by the deposition of amyloid P-peptide (All) plaques in the brain. Full-length amyloid-beta precursor protein (APP) is processed by alpha- and beta-secretases to yield soluble APP derivatives and membrane-bound C-terminal fragments, which are further processed by gamma-secretase to a non-amyloidogenic 3 kDa product or to All fragments. As different A beta fragments contain different parts of the APP transmembrane helix, one may speculate that they are retained more or less efficiently in the membrane. Here, we use the translocon-mediated insertion of different APP-derived polypeptide segments into the endoplasmic reticulum membrane to assess the propensities for membrane retention of All fragments. Our results show a strong correlation between the length of an A beta-derived segment and its ability to integrate into the microsomal membrane.

sted, utgiver, år, opplag, sider
2007. Vol. 581, nr 20, s. 3809-3813
Emneord [en]
amyloid beta-protein precursor, A beta-peptide, translocon mediated, membrane insertion
HSV kategori
Identifikatorer
URN: urn:nbn:se:su:diva-25792DOI: 10.1016/j.febslet.2007.07.003ISI: 000248903600008OAI: oai:DiVA.org:su-25792DiVA, id: diva2:200524
Tilgjengelig fra: 2009-03-19 Laget: 2009-02-20 Sist oppdatert: 2017-12-13bibliografisk kontrollert
Inngår i avhandling
1. Integration and topology of membrane proteins
Åpne denne publikasjonen i ny fane eller vindu >>Integration and topology of membrane proteins
2009 (engelsk)Doktoravhandling, med artikler (Annet vitenskapelig)
Abstract [en]

Membrane proteins comprise around 20-30% of most proteomes. They play important roles in most biochemical pathways. All receptors and ion channels are membrane proteins, which make them attractive targets for drug design. Membrane proteins insert and fold co-translationally into the endoplasmic reticular membrane of eukaryotic cells. The protein-conducting channel that inserts the protein into the membrane is called Sec61 translocon, which is a hetero-oligomeric channel that allows transmembrane segments to insert laterally into the lipid bilayer. The focus of this thesis is how the translocon recognizes the transmembrane helices and integrates them into the membrane.

We have investigated the sequence requirements for the translocon-mediated integration of a transmembrane α-helix into the ER by challenging the Sec61 translocon with designed polypeptide segments in an in vitro expression system that allows a quantitative assessment of membrane insertion efficiency. Our studies suggest that helices might interact with each other already during the membrane-insertion step, possibly forming helical hairpins that partition into the membrane as a single unit. Further, the insertion efficiency for Nin-Cout vs. Nout-Cin transmembrane helices and the integration efficiency of Alzheimer’s Aβ-peptide fragments has been investigated.

Finally, detailed topology mapping was performed on two biologically interesting proteins with unknown topology, the human seipin protein and Drosophila melanogaster odorant receptor OR83b.

sted, utgiver, år, opplag, sider
Stockholm: Institutionen för biokemi och biofysik, 2009. s. 53
Emneord
insertion, Sec61, translocation
HSV kategori
Forskningsprogram
biokemi
Identifikatorer
urn:nbn:se:su:diva-8575 (URN)978-91-7155-827-5 (ISBN)
Disputas
2009-04-09, Magnélisalen, Kemiska övningslaboratoriet, Svante Arrhenius väg 12 A, Stockholm, 10:00 (engelsk)
Opponent
Veileder
Tilgjengelig fra: 2009-03-12 Laget: 2009-02-20 Sist oppdatert: 2016-02-23bibliografisk kontrollert

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