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Archangelo, L.F.* ; Greif, P.A. ; Maucuer, A.* ; Manceau, V.* ; Koneru, N. ; Bigarella, C.L.* ; Niemann, F.* ; dos Santos, M.T.* ; Kobarg, J.* ; Bohlander, S.K. ; Saad, S.T.O.*

The CATS (FAM64A) protein is a substrate of the Kinase Interacting Stathmin (KIS).

Biochim. Biophys. Acta-Mol. Cell Res. 1833, 1269-1279 (2013)
Open Access Green as soon as Postprint is submitted to ZB.
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 (MS or UHMK1) protein as a CATS interacting partner. The interaction between CATS and KIS was confirmed by GST pull-down, co-immunopreciptation 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.
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Publication type Article: Journal article
Document type Scientific Article
Keywords Cats ; Fam64a ; Kis ; Uhmk1 ; Phosphorylation ; Calm/af10-leukemia; Acute Myeloid-leukemia ; Rna-recognition Motif ; Quantitative Phosphoproteomics ; Subcellular-localization ; Up-regulation ; Cell-cycle ; T-all ; Fusion ; Phosphorylation ; Calm-af10
ISSN (print) / ISBN 0167-4889
e-ISSN 1879-2596
Quellenangaben Volume: 1833, Issue: 5, Pages: 1269-1279 Article Number: , Supplement: ,
Publisher Elsevier
Reviewing status Peer reviewed