Characterisation and chromosome mapping of the human non receptor tyrosine kinase gene, brk

Mitchell, Philip J.; Barker, Karen; Shipley, Janet; Crompton, M. R.

doi:10.1038/sj.onc.1201292

Cited by 45 publications

(65 citation statements)

References 34 publications

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“…PTK6 expression is low or undetectable in normal mammary tissues or in benign lesions. However, approximately two-thirds of examined breast tumors express significant levels of PTK6 (3). Elevated expression of PTK6 has also been reported in other cancers, including colon carcinomas (5), prostate carcinomas (6), head and neck cancer (7), oral squamous cell carcinoma (8), and in lymphocytes (9).…”

Section: In the N-terminal Domain Of Arap1 Expression Of Arap1 But mentioning

confidence: 99%

“…Protein tyrosine kinase-6 or PTK6 2 (also known as breast tumor kinase or Brk; Src-related intestinal kinase, or Sik in mice) is a non-receptor tyrosine kinase that is closely related to, but distinct from, the Src family (1)(2)(3)(4). PTK6 expression is low or undetectable in normal mammary tissues or in benign lesions.…”

Section: In the N-terminal Domain Of Arap1 Expression Of Arap1 But mentioning

confidence: 99%

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PTK6 Inhibits Down-regulation of EGF Receptor through Phosphorylation of ARAP1

Kang

Lee

Yoon

et al. 2010

Journal of Biological Chemistry

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Section: In the N-terminal Domain Of Arap1 Expression Of Arap1 But mentioning

confidence: 99%

Section: In the N-terminal Domain Of Arap1 Expression Of Arap1 But mentioning

confidence: 99%

PTK6 Inhibits Down-regulation of EGF Receptor through Phosphorylation of ARAP1

Kang

Lee

Yoon

et al. 2010

Journal of Biological Chemistry

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“…Like rSLM-2, YT521-B interacts with Sam68 and is tyrosinephosphorylated upon overexpression of the tyosine kinases Src and Fyn (26). It remains to be determined whether rSLM-2 is tyrosine-phosphorylated by nuclear tyrosine kinases, such as SIK/BRK, which was shown to phosphorylate Sam68 (64,65).…”

Section: Rslm-2 Interacts With Proteins Involved In Splice Sitementioning

confidence: 99%

The STAR/GSG Family Protein rSLM-2 Regulates the Selection of Alternative Splice Sites

Stoß

Olbrich

Hartmann

et al. 2001

Journal of Biological Chemistry

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We identified the rat Sam68-like mammalian protein (rSLM-2), a member of the STAR (signal transduction and activation of RNA) protein family as a novel splicing regulatory protein. Using the yeast two-hybrid system, coimmunoprecipitations, and pull-down assays, we demonstrate that rSLM-2 interacts with various proteins involved in the regulation of alternative splicing, among them the serine/arginine-rich protein SRp30c, the splicing-associated factor YT521-B and the scaffold attachment factor B. rSLM-2 can influence the splicing pattern of the CD44v5, human transformer-2␤ and tau minigenes in cotransfection experiments. This effect can be reversed by rSLM-2-interacting proteins. Employing rSLM-2 deletion variants, gel mobility shift assays, and linker scan mutations of the CD44 minigene, we show that the rSLM-2-dependent inclusion of exon v5 of the CD44 pre-mRNA is dependent on a short purinerich sequence. Because the related protein of rSLM-2, Sam68, is believed to play a role as an adapter protein during signal transduction, we postulate that rSLM-2 is a link between signal transduction pathways and pre-mRNA processing.Prior to export to the cytosol, pre-mRNA generated from most eukaryotic genes undergoes maturation processes such as splicing, in which intronic sequences are removed and exonic sequences are rejoined, as well as polyadenylation and 5Ј-end capping. There is increasing evidence that transcription, pre-mRNA processing, and RNA transport are coupled in a highly coordinated manner (1-3). Recent results indicate a direct interaction among RNA polymerase II, transcription, capping, splicing, and polyadenylation factors (3-6). These complexes are possibly attached to chromatin, for example by the scaffold attachment factor B (SAF-B 1 ) (7). This supports the model of a large RNA processing unit (8, 9) termed RNA factory (3). Pre-mRNA splicing is characterized by a high fidelity and can be modulated in a cell type-or development-specific way to use exons alternatively. Although the exact mechanisms governing splice site selection are still not fully understood, recent results indicate that loosely defined signals on the pre-mRNA known as splicing enhancers/silencers, play a crucial role in splice site selection (10 -12). An important class of proteins that recognize splicing enhancers/silencers is the serine/arginine-rich (SR) and SR-related protein family that is involved in both constitutive and alternative splicing (13,14). In addition, it has also been shown that an increasing number of heterogenous nuclear ribonucleoproteins (hnRNPs) are involved in the regulation of alternative splicing. For example, splicing regulation of the neuron-specific exon N1 or the src pre-mRNA is under the control of the hnRNPs hnRNP I (polypyrimidine tract binding protein), hnRNP F, and hnRNP H (15, 16). SR proteins and hnRNPs can change alternative splicing patterns in a concentration-dependent manner both in vivo and in vitro (for review, see Refs. 13 and 14). Because the relative expression levels of SR proteins and...

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“…This is supported by the fact that BRK's ability to transform cells is regulated di erently from SRC kinases (Kamalati et al, 1996), together with the ®nding that the structure of the brk gene is distinct from the conserved organisation of the src gene family (Mitchell et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

“…The BRK cDNAs isolated from human breast tumour cells, and used in the functional studies described above, encode a protein identical to that encoded by genomic clones derived from normal human placental DNA (Mitchell et al, 1997). It is therefore possible that the elevation of BRK expression levels alone could have an important functional role during breast tumour development, through imparting on mammary epithelial cells the ability to proliferate in response to limiting concentrations of growth factors such as EGF.…”

Section: Introductionmentioning

confidence: 99%