2004
DOI: 10.1074/jbc.m409579200
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The Nuclear Tyrosine Kinase BRK/Sik Phosphorylates and Inhibits the RNA-binding Activities of the Sam68-like Mammalian Proteins SLM-1 and SLM-2

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Cited by 79 publications
(91 citation statements)
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“…In normal breast epithelium, PTK6 is low or undetectable, but the protein is overexpressed in many breast carcinomas (Petro et al, 2004;Zhang et al, 2005), suggesting, PTK6 expression is related to carcinogenesis. In contrast, high levels of PTK6 are expressed in some differentiating epithelial tissues such as normal gastrointestinal tract, skin (Llor et al, 1999;Haegebarth et al, 2004), and prostate (Derry et al, 2003), and PTK6 expression was associated with the degree of differentiation of breast tissue as indicated by ER expression (Zhao et al, 2003). The correlation of PTK6 protein expression with the histological tumour grade observed in our study may also support an association between PTK6 and cell differentiation.…”
Section: Discussionsupporting
confidence: 51%
“…In normal breast epithelium, PTK6 is low or undetectable, but the protein is overexpressed in many breast carcinomas (Petro et al, 2004;Zhang et al, 2005), suggesting, PTK6 expression is related to carcinogenesis. In contrast, high levels of PTK6 are expressed in some differentiating epithelial tissues such as normal gastrointestinal tract, skin (Llor et al, 1999;Haegebarth et al, 2004), and prostate (Derry et al, 2003), and PTK6 expression was associated with the degree of differentiation of breast tissue as indicated by ER expression (Zhao et al, 2003). The correlation of PTK6 protein expression with the histological tumour grade observed in our study may also support an association between PTK6 and cell differentiation.…”
Section: Discussionsupporting
confidence: 51%
“…In normal breast epithelium, PTK6 expression is low or undetectable, but it is elevated in many breast carcinomas (Petro et al, 2004;Zhang et al, 2005;Aubele et al, 2007), indicating that PTK6 overexpression may be related to carcinogenesis. In contrast, high levels of PTK6 are expressed in some differentiating epithelial tissues, such as normal gastrointestinal tract, skin (Llor et al, 1999;Haegebarth et al, 2004), and prostate (Derry et al, 2003). Moreover, PTK6 expression is associated with the degree of differentiation of breast tissue as indicated by oestrogen receptor (ER) expression (Zhao et al, 2003).…”
mentioning
confidence: 99%
“…In recent years, several additional PTK6 substrates have been identified (Derry et al, 2000;Babic et al, 2004;Haegebarth et al, 2004Haegebarth et al, , 2005. The first reported substrate of PTK6 phosphorylation was Sam68 (Src-associated in mitosis 68 kDa), and it was shown that PTK6 negatively regulates its RNA-binding activity (Derry et al, 2000).…”
mentioning
confidence: 99%
“…BRK expression suppressed cell proliferation through EGFR-mediated phosphorylation of Sam68 in a human breast cancer cell line (Coyle et al, 2003;Derry et al, 2000;Lukong et al, 2005). Similarly, BRK phosphorylates the Sam68-like mammalian proteins, SLM-1 and SLM-2, and negatively regulates their RNA-binding functions (Haegebarth et al, 2004). Downstream of EGFR, PSF is a BRK substrate, and this tyrosine phosphorylation of PSF induces cytoplasmic relocalization, impairment of its binding to polypyrimidine RNA, and cell cycle arrest (Lukong et al, 2009).…”
Section: Substrates Interacting Proteins and Activationmentioning
confidence: 99%
“…BRK substrates include RNA-binding proteins (Sam68 (Coyle et al, 2003;Derry et al, 2000;Lukong et al, 2005), SLM-1/2 (Haegebarth et al, 2004), and the polypyrimidine tractbinding protein-associated splicing factor (PSF) (Lukong et al, 2009)), transcription factors (STAT3 (Liu et al, 2006) and STAT5A/B (Weaver and Silva, 2007)), adaptor molecules (STAP-2) (Mitchell et al, 2000), and a variety of signaling molecules (paxillin (Chen et al, 2004), p190RhoGAP (Shen et al, 2008), kinesin-associated protein 3A (KAP3A) (Lukong and Richard, 2008), Akt (Zhang et al, 2005), -catenin (Palka-Hamblin et al, 2010), and ARAP1 (Arf-GAP, Rho-GAP, ankyrin repeat and PH domain-containing protein 1; also known as centaurin δ-2) (Kang et al, 2010)). Although BRK expression is known to induce tyrosine phosphorylation in some of these, similar actions in others have yet to be confirmed.…”
Section: Substrates Interacting Proteins and Activationmentioning
confidence: 99%