Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/200501
Type: Artigo de periódico
Title: The Cats (fam64a) Protein Is A Substrate Of The Kinase Interacting Stathmin (kis).
Author: Archangelo, Leticia Fröhlich
Greif, Philipp A
Maucuer, Alexandre
Manceau, Valérie
Koneru, Naresh
Bigarella, Carolina L
Niemann, Fernanda
dos Santos, Marcos Tadeu
Kobarg, Jörg
Bohlander, Stefan K
Saad, Sara Teresinha Olalla
Abstract: The CATS protein (also known as FAM64A and RCS1) was first identified as a novel CALM (PICALM) interactor that influences the subcellular localization of the leukemogenic fusion protein CALM/AF10. CATS is highly expressed in cancer cell lines in a cell cycle dependent manner and is induced by mitogens. CATS is considered a marker for proliferation, known to control the metaphase-to-anaphase transition during the cell division. Using CATS as a bait in a yeast two-hybrid screen we identified the Kinase Interacting Stathmin (KIS or UHMK1) protein as a CATS interacting partner. The interaction between CATS and KIS was confirmed by GST pull-down, co-immunoprecipitation and co-localization experiments. Using kinase assay we showed that CATS is a substrate of KIS and mapped the phosphorylation site to CATS serine 131 (S131). Protein expression analysis revealed that KIS levels changed in a cell cycle-dependent manner and in the opposite direction to CATS levels. In a reporter gene assay KIS was able to enhance the transcriptional repressor activity of CATS, independent of CATS phophorylation at S131. Moreover, we showed that CATS and KIS antagonize the transactivation capacity of CALM/AF10.In summary, our results show that CATS interacts with and is a substrate for KIS, suggesting that KIS regulates CATS function.
Subject: Binding Sites
Carrier Proteins
Gene Expression Regulation, Neoplastic
Hek293 Cells
Humans
Immunoprecipitation
Intracellular Signaling Peptides And Proteins
Oncogene Proteins, Fusion
Phosphorylation
Protein Binding
Protein Interaction Maps
Protein-serine-threonine Kinases
Rights: fechado
Identifier DOI: 10.1016/j.bbamcr.2013.02.004
Address: http://www.ncbi.nlm.nih.gov/pubmed/23419774
Date Issue: 2013
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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