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

Abstract

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 Kuźnicki 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.

Comparative proteomic profiling reveals aberrant cell proliferation in the brain of embryonic Ts1Cje, a mouse model of Down syndrome

“…detected in MALDI-TOF MS analysis. CACYBP interacts with not only S100A6 but also some calcium-binding proteins of the S100 family (S100A1, S100A12, S100B, and S100P) (Filipek et al, 2002), S-phase kinase-associated protein 1 (Matsuzawa and Reed, 2001), tubulin (Schneider et al, 2010), and ERK1/2 (Kilanczyk et al, 2009) and takes part in diverse cellular processes such as ubiquitination, proliferation, differentiation, tumorigenesis, cytoskeletal rearrangement, or regulation of transcription through interaction with these target proteins (Schneider and Filipek, 2011). Increased levels of CACYBP during differentiation and high levels of CACYBP in brain neurons indicate that CACYBP may be involved in differentiation of neuronal cells (Jastrzebska et al, 2000;Filipek et al, 2002).…”

Relationship between CacyBP/SIP expression and prognosis in astrocytoma

“…It was originally discovered as an S100A6 (calcyclin) target and later as a Siah-1 interacting protein, and it mediates ubiquitination and the b-catenin degradation pathway. [1][2][3][4][5] Subsequent studies examined CacyBP/SIP expression in normal and tumor tissues in humans. Increasing evidence suggests that CacyBP/SIP has roles in many cellular processes, such as differentiation, proliferation, tumorigenesis, cytoskeletal rearrangement, transcription regulation and ubiquitination.…”

“…Increasing evidence suggests that CacyBP/SIP has roles in many cellular processes, such as differentiation, proliferation, tumorigenesis, cytoskeletal rearrangement, transcription regulation and ubiquitination. 5 Astrocytoma is the most frequently occurring primary brain tumor, and is classified by the World Health Organization (WHO) system as: grade I, pilocytic astrocytoma; grade II, diffuse astrocytoma; grade III, anaplastic astrocytoma; and grade IV, glioblastoma multiforme (GBM). 6 The WHO grades I to II astrocytomas are regarded as low-grade and grades III to IV as high-grade astrocytomas.…”

S100 family signaling network and related proteins in pancreatic cancer (Review)

“…S100A6. The S100A6 gene is a single-copy gene, located on human chromosome lq21, adjacent to ski proto-oncogene (74). S100A6 consists of 90 amino acids.…”