Search: onr:"swepub:oai:gup.ub.gu.se/116964" >
A brain-specific is...
A brain-specific isoform of mitochondrial apoptosis-inducing factor: AIF2.
-
Hangen, E (author)
-
De Zio, D (author)
-
Bordi, M (author)
-
show more...
-
- Zhu, Changlian, 1964 (author)
- Gothenburg University,Göteborgs universitet,Institutionen för neurovetenskap och fysiologi, sektionen för klinisk neurovetenskap och rehabilitering,Institute of Neuroscience and Physiology, Department of Clinical Neuroscience and Rehabilitation
-
Dessen, P (author)
-
Caffin, F (author)
-
Lachkar, S (author)
-
Perfettini, J-L (author)
-
Lazar, V (author)
-
Benard, J (author)
-
Fimia, G M (author)
-
Piacentini, M (author)
-
Harper, F (author)
-
Pierron, G (author)
-
Vicencio, J M (author)
-
Bénit, P (author)
-
de Andrade, A (author)
-
Höglinger, G (author)
-
Culmsee, C (author)
-
Rustin, P (author)
-
- Blomgren, Klas, 1963 (author)
- Gothenburg University,Göteborgs universitet,Institutionen för kliniska vetenskaper, Avdelningen för pediatrik,Institute of Clinical Sciences, Department of Pediatrics
-
Cecconi, F (author)
-
Kroemer, G (author)
-
Modjtahedi, N (author)
-
show less...
-
(creator_code:org_t)
- 2010-01-29
- 2010
- English.
-
In: Cell death and differentiation. - : Springer Science and Business Media LLC. - 1476-5403 .- 1350-9047. ; 17:7, s. 1155-66
- Related links:
-
https://www.nature.c...
-
show more...
-
https://gup.ub.gu.se...
-
https://doi.org/10.1...
-
show less...
Abstract
Subject headings
Close
- Apoptosis-inducing factor (AIF) has important supportive as well as potentially lethal roles in neurons. Under normal physiological conditions, AIF is a vital redox-active mitochondrial enzyme, whereas in pathological situations, it translocates from mitochondria to the nuclei of injured neurons and mediates apoptotic chromatin condensation and cell death. In this study, we reveal the existence of a brain-specific isoform of AIF, AIF2, whose expression increases as neuronal precursor cells differentiate. AIF2 arises from the utilization of the alternative exon 2b, yet uses the same remaining 15 exons as the ubiquitous AIF1 isoform. AIF1 and AIF2 are similarly imported to mitochondria in which they anchor to the inner membrane facing the intermembrane space. However, the mitochondrial inner membrane sorting signal encoded in the exon 2b of AIF2 is more hydrophobic than that of AIF1, indicating a stronger membrane anchorage of AIF2 than AIF1. AIF2 is more difficult to be desorbed from mitochondria than AIF1 on exposure to non-ionic detergents or basic pH. Furthermore, AIF2 dimerizes with AIF1, thereby preventing its release from mitochondria. Conversely, it is conceivable that a neuron-specific AIF isoform, AIF2, may have been 'designed' to be retained in mitochondria and to minimize its potential neurotoxic activity.Cell Death and Differentiation advance online publication, 29 January 2010; doi:10.1038/cdd.2009.211.
Publication and Content Type
- ref (subject category)
- art (subject category)
Find in a library
To the university's database
- By the author/editor
-
Hangen, E
-
De Zio, D
-
Bordi, M
-
Zhu, Changlian, ...
-
Dessen, P
-
Caffin, F
-
show more...
-
Lachkar, S
-
Perfettini, J-L
-
Lazar, V
-
Benard, J
-
Fimia, G M
-
Piacentini, M
-
Harper, F
-
Pierron, G
-
Vicencio, J M
-
Bénit, P
-
de Andrade, A
-
Höglinger, G
-
Culmsee, C
-
Rustin, P
-
Blomgren, Klas, ...
-
Cecconi, F
-
Kroemer, G
-
Modjtahedi, N
-
show less...
- Articles in the publication
-
Cell death and d ...
- By the university
-
University of Gothenburg