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Interactions of an Arabidopsis RanBPM homologue with LisH-CTLH domain proteins revealed high conservation of CTLH complexes in eukaryotes

SYSNO ASEP	0380982
Document Type	J - Journal Article
R&D Document Type	Journal Article
Subsidiary J	Článek ve WOS
Title	Interactions of an Arabidopsis RanBPM homologue with LisH-CTLH domain proteins revealed high conservation of CTLH complexes in eukaryotes
Author(s)	Tomaštíková, Eva (UEB-Q)_{RID, ORCID} Cenklová, Věra (UEB-Q) Kohoutová, Lucie (MBU-M)_RID Petrovská, Beáta (UEB-Q)_{RID, ORCID} Váchová, Lenka (UEB-Q) Halada, Petr (MBU-M)_{RID, ORCID} Kočárová, Gabriela (MBU-M) Binarová, Pavla (MBU-M)_{RID, ORCID}
Source Title	BMC Plant Biology. - : BioMed Central - ISSN 1471-2229 Roč. 12, č. 83 (2012)
Number of pages	14 s.
Language	eng - English
Country	GB - United Kingdom
Keywords	Arabidopsis homologue of RanBPM ; CTLH-complex ; LisH-CTLH domain proteins
Subject RIV	EB - Genetics ; Molecular Biology
R&D Projects	GA204/07/1169 GA ČR - Czech Science Foundation (CSF)
	GP204/09/P155 GA ČR - Czech Science Foundation (CSF)
	GAP501/12/2333 GA ČR - Czech Science Foundation (CSF)
	LC06034 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
	LC545 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
	IAA500200719 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR)
CEZ	AV0Z50380511 - UEB-Q (2005-2011)
	AV0Z50200510 - MBU-M (2005-2011)
UT WOS	000307098700001
DOI	10.1186/1471-2229-12-83
Annotation	Based on sequence similarity, we identified a homologue of the human RanBPM in Arabidopsis thaliana. AtRanBPM protein has highly conserved SPRY, LisH, CTLH and CRA domains. Cell fractionation showed that endogenous AtRanBPM or expressed GFP-AtRanBPM are mainly cytoplasmic proteins with only a minor portion detectable in microsomal fractions. AtRanBPM was identified predominantly in the form of soluble cytoplasmic complexes similar to 230 - 500 kDa in size. Immunopurification of AtRanBPM followed by mass spectrometric analysis identified proteins containing LisH and CRA domains; LisH, CRA, RING-U-box domains and a transducin/WD40 repeats in a complex with AtRanBPM. Homologues of identified proteins are known to be components of the C-terminal to the LisH motif (CTLH) complexes in humans and budding yeast. Microscopic analysis of GFP-AtRanBPM in vivo and immunofluorescence localization of endogenous AtRanBPM protein in cultured cells and seedlings of Arabidopsis showed mainly cytoplasmic and nuclear localization. Absence of colocalization with.-tubulin was consistent with the biochemical data and suggests another than a centrosomal role of the AtRanBPM protein. Conclusion: We showed that as yet uncharacterized Arabidopsis RanBPM protein physically interacts with LisH-CTLH domain-containing proteins. The newly identified high molecular weight cytoplasmic protein complexes of AtRanBPM showed homology with CTLH types of complexes described in mammals and budding yeast. Although the exact functions of the CTLH complexes in scaffolding of protein degradation, in protein interactions and in signalling from the periphery to the cell centre are not yet fully understood, structural conservation of the complexes across eukaryotes suggests their important biological role.
Workplace	Institute of Experimental Botany
Contact	David Klier, knihovna@ueb.cas.cz, Tel.: 220 390 469
Year of Publishing	2013

Number of the records: 1