LPP (gene)
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Gene ontology | |||
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| View/Edit Human | View/Edit Mouse |
 | This 'further reading' section may need cleanup. (January 2020) ) |
Lipoma-preferred partner is a protein that in humans is encoded by the LPP gene.[5][6]
Function
Lipoma-preferred partner is a subfamily of LIM domain proteins that are characterized by an N-terminal proline rich region and three C-terminal LIM domains. The encoded protein localizes to the cell periphery in focal adhesions and may be involved in cell-cell adhesion and cell motility. This protein also shuttles through the nucleus and may function as a transcriptional co-activator. This gene is located at the junction of certain disease related chromosomal translocations which result in the expression of fusion proteins that may promote tumor growth.[6]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000145012 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000033306 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- PMID 8812423.
- ^ a b "Entrez Gene: LPP LIM domain containing preferred translocation partner in lipoma".
Further reading
- Schoenmakers EF, Wanschura S, Mols R, et al. (1995). "Recurrent rearrangements in the high mobility group protein gene, HMGI-C, in benign mesenchymal tumours". Nat. Genet. 10 (4): 436–44. S2CID 29935721.
- Petit MM, Swarts S, Bridge JA, Van de Ven WJ (1998). "Expression of reciprocal fusion transcripts of the HMGIC and LPP genes in parosteal lipoma". Cancer Genet. Cytogenet. 106 (1): 18–23. PMID 9772904.
- Petit MM, Fradelizi J, Golsteyn RM, et al. (2000). "LPP, an Actin Cytoskeleton Protein Related to Zyxin, Harbors a Nuclear Export Signal and Transcriptional Activation Capacity". Mol. Biol. Cell. 11 (1): 117–29. PMID 10637295.
- Rogalla P, Lemke I, Kazmierczak B, Bullerdiek J (2001). "An identical HMGIC-LPP fusion transcript is consistently expressed in pulmonary chondroid hamartomas with t(3;12)(q27-28;q14-15)". Genes Chromosomes Cancer. 29 (4): 363–6. S2CID 35883889.
- Harrington JJ, Sherf B, Rundlett S, et al. (2001). "Creation of genome-wide protein expression libraries using random activation of gene expression". Nat. Biotechnol. 19 (5): 440–5. S2CID 25064683.
- Dahéron L, Veinstein A, Brizard F, et al. (2001). "Human LPP gene is fused to MLL in a secondary acute leukemia with a t(3;11) (q28;q23)". Genes Chromosomes Cancer. 31 (4): 382–9. S2CID 32921978.
- Lemke I, Rogalla P, Bullerdiek J (2002). "A novel LPP fusion gene indicates the crucial role of truncated LPP proteins in lipomas and pulmonary chondroid hamartomas". Cytogenet. Cell Genet. 95 (3–4): 153–6. S2CID 42951388.
- Petit MM, Meulemans SM, Van de Ven WJ (2003). "The focal adhesion and nuclear targeting capacity of the LIM-containing lipoma-preferred partner (LPP) protein". J. Biol. Chem. 278 (4): 2157–68. PMID 12441356.
- Lemke I, Rogalla P, Grundmann F, et al. (2003). "Expression of the HMGA2-LPP fusion transcript in only 1 of 61 karyotypically normal pulmonary chondroid hamartomas". Cancer Genet. Cytogenet. 138 (2): 160–4. PMID 12505264.
- Salomon AR, Ficarro SB, Brill LM, et al. (2003). "Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry". Proc. Natl. Acad. Sci. U.S.A. 100 (2): 443–8. PMID 12522270.
- Li B, Zhuang L, Reinhard M, Trueb B (2003). "The lipoma preferred partner LPP interacts with alpha-actinin". J. Cell Sci. 116 (Pt 7): 1359–66. PMID 12615977.
- Gorenne I, Nakamoto RK, Phelps CP, et al. (2003). "LPP, a LIM protein highly expressed in smooth muscle". Am. J. Physiol., Cell Physiol. 285 (3): C674–85. PMID 12760907.
- Brill LM, Salomon AR, Ficarro SB, et al. (2004). "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry". Anal. Chem. 76 (10): 2763–72. PMID 15144186.
- Rush J, Moritz A, Lee KA, et al. (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nat. Biotechnol. 23 (1): 94–101. S2CID 7200157.
- Petit MM, Meulemans SM, Alen P, et al. (2006). "The tumor suppressor Scrib interacts with the zyxin-related protein LPP, which shuttles between cell adhesion sites and the nucleus". BMC Cell Biol. 6 (1): 1. PMID 15649318.
- Zhang Y, Wolf-Yadlin A, Ross PL, et al. (2005). "Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules". Mol. Cell. Proteomics. 4 (9): 1240–50. PMID 15951569.
- Tao WA, Wollscheid B, O'Brien R, et al. (2005). "Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry". Nat. Methods. 2 (8): 591–8. S2CID 20475874.
- von Ahsen I, Rogalla P, Bullerdiek J (2006). "Expression patterns of the LPP-HMGA2 fusion transcript in pulmonary chondroid hamartomas with t(3;12)(q27 approximately 28;q14 approximately 15)". Cancer Genet. Cytogenet. 163 (1): 68–70. PMID 16271958.
- Kubo T, Matsui Y, Goto T, et al. (2006). "Overexpression of HMGA2-LPP fusion transcripts promotes expression of the alpha 2 type XI collagen gene". Biochem. Biophys. Res. Commun. 340 (2): 476–81. PMID 16375854.
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