NDLI: Analysis of nuclear protein complexes comprising α-actinin-4 by 2D-electrophoresis and mass spectrometry

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Analysis of nuclear protein complexes comprising α-actinin-4 by 2D-electrophoresis and mass spectrometry

Content Provider	Springer Nature Link
Author	Khotin, M. G. Turoverova, L. V. Podolskaya, E. P. Krasv, I. A. Solovyeva, A. V. Akseva, V. Yu. Magnusson, K. E. Pinaev, G. P. Tentler, D. G.
Copyright Year	2009
Abstract	Actin-binding protein α-actinin-4 is a member of the spectrin superfamily; it is located in both the cytoplasm and nucleus. However, nuclear functions of α-actinin-4 are still not clear. In this study, we analyzed the composition of nuclear protein complexes associated with α-actinin-4 in A431 cells. Using 2D electrophoresis, we found that about 50 different proteins may be associated with nuclear α-actinin-4. Major proteins of these complexes were analyzed by mass spectrometry and the following proteins have been identified: β-actin, α- and β-tubulins, ribonucleoprotein A2/B1 (regulates splicing and is associated with β-actin), peroxiredoxin-1 (involved in oxidative stress), and glycolytic enzyme D-3-phosphoglycerate dehydrogenase. The detection of these proteins in nuclear complexes with α-actinin-4 may suggest that α-actinin-4 is implicated in transcription and splicing. The presence of β-actin in these complexes was confirmed by tandem mass spectrometry (MALDI-TOF-TOF). The immunoprecipitation of nuclear proteins with antibodies against α-tubulin proved the association of α-actinin-4 with α-tubulin in the protein complex. Nuclear α-actinin-4 consists of a 105-kDa, full-size isoform and two truncated isoforms of 65 and 75 kDa; only truncated isoforms have been found in nuclear complexes with α-tubulin. These data suggest that α-actinin-4 is associated with a number of various nuclear protein complexes that may be able to carry out different functions in the cell nucleus.
Starting Page	431
Ending Page	437
Page Count	7
File Format	PDF
ISSN	1990519X
Journal	Cell and Tissue Biology
Volume Number	3
Issue Number	5
e-ISSN	19905203
Language	English
Publisher	SP MAIK Nauka/Interperiodica
Publisher Date	2009-11-05
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	α-actinin-4 mass spectrometry Cell Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology

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Analysis of nuclear protein complexes comprising α-actinin-4 by 2D-electrophoresis and mass spectrometry

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Analysis of nuclear protein complexes comprising α-actinin-4 by 2D-electrophoresis and mass spectrometry