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Amino Acids. 2011 Oct;41(4):773-80. doi: 10.1007/s00726-010-0498-2. Epub 2010 Feb 25.

S100A6 binding protein and Siah-1 interacting protein (CacyBP/SIP): spotlight on properties and cellular function.

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  • 1Nencki Institute of Experimental Biology, 3 Pasteur Street, 02-093, Warsaw, Poland.


The CacyBP/SIP protein (S100A6 binding protein and Siah-1 interacting protein) was originally discovered in Ehrlich ascites tumor cells as a S100A6 (calcyclin) target (Filipek and Wojda in Biochem J 320:585-587, 1996; Filipek and Ku┼║nicki in J Neurochem 70(5):1793-1798, 1998) and later on as a Siah-1 interacting protein (Matsuzawa and Reed in Mol Cell 7(5):915-926, 2001). CacyBP/SIP binds several target proteins such as some calcium binding proteins of the S100 family (Filipek et al. in J Biol Chem 277(32):28848-28852, 2002), Skp1 (Matsuzawa and Reed in Mol Cell 7(5):915-926, 2001), tubulin (Schneider et al. in Biochim Biophys Acta 1773(11):1628-1636, 2007) and ERK1/2 (Kilanczyk et al. in Biochem Biophys Res Commun 380:54-59, 2009). Studies concerning distribution of CacyBP/SIP show that it is present in various tissues and that a particularly high level of CacyBP/SIP is observed in brain (Jastrzebska et al. in J Histochem Cytochem 48(9):1195-1202, 2000). Regarding the function of CacyBP/SIP, there are some reports suggesting its role in cellular processes such as ubiquitination, proliferation, differentiation, tumorigenesis, cytoskeletal rearrangement or regulation of transcription. This review describes the properties of CacyBP/SIP and summarizes all findings concerning its cellular function.

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