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Neutron reflectomet...
Neutron reflectometry and NMR spectroscopy of full-length Bcl-2 protein reveal its membrane localization and conformation
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- Ul Mushtaq, Ameeq (author)
- Umeå universitet,Umeå University,Kemiska institutionen
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- Ådén, Jörgen, 1980- (author)
- Umeå universitet,Umeå University,Kemiska institutionen
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- Clifton, L. A. (author)
- ISIS Neutron and Muon Source
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- Wacklin-Knecht, Hanna (author)
- Lund University,Lunds universitet,Fysikalisk kemi,Enheten för fysikalisk och teoretisk kemi,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Physical Chemistry,Physical and theoretical chemistry,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH,European Spallation Source ERIC, Denmark
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- Campana, M. (author)
- ISIS Neutron and Muon Source
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- Dingeldein, Artur P. G. (author)
- Umeå universitet,Umeå University,Kemiska institutionen
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- Persson, Cecilia, 1974 (author)
- University of Gothenburg,Gothenburg University,Göteborgs universitet,Svenskt NMR-centrum vid Göteborgs universitet,Swedish NMR Centre at Göteborg University
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- Sparrman, Tobias (author)
- Umeå universitet,Umeå University,Kemiska institutionen
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Grobner, G. (author)
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(creator_code:org_t)
- 2021-04-27
- 2021
- English.
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In: Communications Biology. - : Springer Science and Business Media LLC. - 2399-3642. ; 4:1
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Abstract
Subject headings
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- B-cell lymphoma 2 (Bcl-2) proteins are the main regulators of mitochondrial apoptosis. Anti-apoptotic Bcl-2 proteins possess a hydrophobic tail-anchor enabling them to translocate to their target membrane and to shift into an active conformation where they inhibit pro-apoptotic Bcl-2 proteins to ensure cell survival. To address the unknown molecular basis of their cell-protecting functionality, we used intact human Bcl-2 protein natively residing at the mitochondrial outer membrane and applied neutron reflectometry and NMR spectroscopy. Here we show that the active full-length protein is entirely buried into its target membrane except for the regulatory flexible loop domain (FLD), which stretches into the aqueous exterior. The membrane location of Bcl-2 and its conformational state seems to be important for its cell-protecting activity, often infamously upregulated in cancers. Most likely, this situation enables the Bcl-2 protein to sequester pro-apoptotic Bcl-2 proteins at the membrane level while sensing cytosolic regulative signals via its FLD region. Through neutron reflectometry and NMR spectroscopy studies, Mushtaq et al study the full-length Bcl-2 protein reconstituted in lipid bilayers. They find that, in contrast to previously studied truncated, soluble protein versions, intact Bcl-2 is mainly embedded in the membrane with its regulatory loop highly flexible.
Subject headings
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Cell- och molekylärbiologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Cell and Molecular Biology (hsv//eng)
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Keyword
- lipid-membranes
- family
- bax
- apoptosis
- mitochondria
- dynamics
- xl
- insertion
- bcl-x(l)
- software
- Life Sciences & Biomedicine - Other Topics
- Science & Technology - Other
- Topics
Publication and Content Type
- ref (subject category)
- art (subject category)
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- By the author/editor
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Ul Mushtaq, Amee ...
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Ådén, Jörgen, 19 ...
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Clifton, L. A.
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Wacklin-Knecht, ...
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Campana, M.
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Dingeldein, Artu ...
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show more...
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Persson, Cecilia ...
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Sparrman, Tobias
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Grobner, G.
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show less...
- About the subject
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- MEDICAL AND HEALTH SCIENCES
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MEDICAL AND HEAL ...
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and Basic Medicine
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and Cell and Molecul ...
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
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and Biochemistry and ...
- Articles in the publication
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Communications B ...
- By the university
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University of Gothenburg
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Lund University
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Umeå University