Sandbox Reserved 168: Difference between revisions
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== Structure == | == Structure == | ||
This protein is made up of 728 amino acids<ref name="structure"> Wilson JJ, Malakhova M, Zhang R, Joachimiak A, Hedge RS. May 2004. "Crystal Struture of the Dachshund homology domain of human SKI" Structure 12 (5):785-92. http://www.ncbi.nlm.nih.gov/pubmed/15130471 </ref>. The SKI protein maintains several domains that include the amino-terminus, a proline rich area, helix-loop-helix motifs, a cysteine/histidine-rich area, a region of basic amino acids and finally a leucine zipper-like domain<ref name="Zheng"> Zheng G, Teumer J, Colmenares C, Richmond C and Stavnezer E. 1997. Oncogene. http://www.nature.com/onc/journal/v22/n20/full/1206452a.html</ref>. | This protein is made up of 728 amino acids<ref name="structure"> Wilson JJ, Malakhova M, Zhang R, Joachimiak A, Hedge RS. May 2004. "Crystal Struture of the Dachshund homology domain of human SKI" Structure 12 (5):785-92. http://www.ncbi.nlm.nih.gov/pubmed/15130471 </ref>. The SKI protein maintains several domains that include the amino-terminus, a proline rich area, helix-loop-helix motifs, a cysteine/histidine-rich area, a region of basic amino acids and finally a leucine zipper-like domain<ref name="Zheng"> Zheng G, Teumer J, Colmenares C, Richmond C and Stavnezer E. 1997. Oncogene. http://www.nature.com/onc/journal/v22/n20/full/1206452a.html</ref>. SKI has been currently assigned to chromosome 1p36, a common region of alteration in human cancers including melanomas. | ||
== Function == | == Function == | ||
SKI, as mentioned before is an oncoprotein that represses TGF-beta and nuclear receptor signaling. It is involved in the regulation of cellular transformation and differentiation. The SKI protein has been associated with tumors at large levels of cellular concentrations and it has been shown to interfere with normal cellular functioning. It was recently | SKI, as mentioned before is an oncoprotein that represses TGF-beta and nuclear receptor signaling. It is involved in the regulation of cellular transformation and differentiation. The SKI protein has been associated with tumors at large levels of cellular concentrations and it has been shown to interfere with normal cellular functioning. It was recently discovered that SKI plays a role not only inside the nucleus but also outside of the nucleus in the cytoplasm. | ||
== Clinical Applications == | == Clinical Applications == | ||
Revision as of 04:33, 30 March 2011
SKI proteinSKI protein
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| This Sandbox is Reserved from March 9, 2011, through May 30, 2011 for use by the course Biochemistry at Reinhardt University, Waleska, USA, taught by Irma Santoro. This reservation includes Sandbox Reserved 162 through Sandbox Reserved 168. |
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BackgroundBackground
The SKI protein was first identified as an oncoprotein. An oncoprotein is one that has the potential to cause abnormal cellular proliferation if mutated or if expressed in quantitative amounts. Although, for a time the method by which the SKI protein acquired such capabilities was unknown, it was recently discovered that SKI interacts with smad after stimulation by TGF-beta. TGF-beta are proteins directly associated with proliferation and cellular differentiation, while smads are transcription factors that transduce transforming growth factor-betar(TGF-beta) members to activate transcription. SKI blocks the activation of transcription witht eh smad complexes which makes the cells resistant to the inhibitory reactions of normal growth induced by TGF-beta. Note that the stimulation of TGF-beta may cause the rapid degradation of SKI. However, after a relatively brief amount of time its expression is strongly induced. [1].
StructureStructure
This protein is made up of 728 amino acids[2]. The SKI protein maintains several domains that include the amino-terminus, a proline rich area, helix-loop-helix motifs, a cysteine/histidine-rich area, a region of basic amino acids and finally a leucine zipper-like domain[3]. SKI has been currently assigned to chromosome 1p36, a common region of alteration in human cancers including melanomas.
FunctionFunction
SKI, as mentioned before is an oncoprotein that represses TGF-beta and nuclear receptor signaling. It is involved in the regulation of cellular transformation and differentiation. The SKI protein has been associated with tumors at large levels of cellular concentrations and it has been shown to interfere with normal cellular functioning. It was recently discovered that SKI plays a role not only inside the nucleus but also outside of the nucleus in the cytoplasm.
Clinical ApplicationsClinical Applications
SKI has been linked to various types of cancer such as melanoma, esophageal cell carcinoma, cervical cancer and the process of tumor progresssion. The SKI oncoprotein has been demonstrated to assist tyrosine kinases to cause leukemia, recently it has been demonstrated that the protein also plays a regulatory role in several signal transduction pathways that are frequent targets for mutagenesis in human tumors.
ReferencesReferences
- ↑ Reed JA, Lin Q, Chen D, Mian IS, Medrano EE. SKI Pathways Inducing Progression of Human Melanoma. June 2005. http://www.ncbi.nlm.nih.gov/pubmed/15986136
- ↑ Wilson JJ, Malakhova M, Zhang R, Joachimiak A, Hedge RS. May 2004. "Crystal Struture of the Dachshund homology domain of human SKI" Structure 12 (5):785-92. http://www.ncbi.nlm.nih.gov/pubmed/15130471
- ↑ Zheng G, Teumer J, Colmenares C, Richmond C and Stavnezer E. 1997. Oncogene. http://www.nature.com/onc/journal/v22/n20/full/1206452a.html