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The nucleolar PICT-1/GLTSCR2 protein forms homo-oligomers.

Abstract：

:The human "protein interacting with carboxyl terminus 1" (PICT-1), also designated as the "glioma tumor suppressor candidate region 2 gene product", GLTSCR2, is a nucleolar protein whose activity is, as yet, unknown. Contradictory results regarding the role of PICT-1 in cancer have been reported, and PICT-1 has been suggested to function either as a tumor suppressor protein or as an oncogene. In this study, we demonstrate self-association of PICT-1. Through yeast two-hybrid assay, we identified PICT-1 as its own interaction partner. We confirmed the interaction of PICT-1 with itself by direct yeast two-hybrid assay and also showed self-association of PICT-1 in mammalian cells by co-immunoprecipitation and fluorescence resonance energy transfer assays. Furthermore, we confirmed direct self-association of PICT-1 by using in vitro microfluidic affinity binding assays. The later assay also identified the carboxy-terminal domain as mediating self-interaction of PICT-1. Glutaraldehyde cross-linking and gel-filtration assays suggest that PICT-1 forms dimers, though it may form higher-order complexes as well. Our findings add another layer of complexity in understanding the different functions of PICT-1 and may help provide insights regarding the activities of this protein.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Borodianskiy-Shteinberg T,Kalt I,Kipper S,Nachum N,Katz S,Pauker MH,Barda-Saad M,Gerber D,Sarid R

doi

10.1016/j.jmb.2014.04.006

subject

Has Abstract

pub_date

2014-06-12 00:00:00

pages

2363-78

issue

12

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(14)00181-8

journal_volume

426

pub_type

杂志文章

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