PITPNM1

Membrane-associated phosphatidylinositol transfer protein 1 is a protein that in humans is encoded by the PITPNM1 gene.[4][5]

PITPNM1
Identifiers
Aliases	PITPNM1, DRES9, NIR2, PITPNM, RDGB, RDGB1, RDGBA, RDGBA1, Rd9, phosphatidylinositol transfer protein membrane associated 1
External IDs	OMIM: 608794 MGI: 1197524 HomoloGene: 3608 GeneCards: PITPNM1
Gene location (Human) Chr. Chromosome 11 (human)[1] Band 11q13.2 Start 67,491,768 bp[1] End 67,506,263 bp[1]
RNA expression pattern More reference expression data
Gene ontology Molecular function • GO:0001948 protein binding • metal ion binding • phosphatidylinositol transporter activity • phosphatidylcholine binding • phosphatidylinositol binding • phosphatidic acid binding • phospholipid transporter activity • calcium ion binding • receptor tyrosine kinase binding • phosphatidylcholine transporter activity Cellular component • Golgi cisterna membrane • lipid droplet • Golgi apparatus • midbody • cleavage furrow • intracellular • endoplasmic reticulum membrane • membrane • endoplasmic reticulum • cytoplasm • cytosol • cytoplasmic ribonucleoprotein granule • microtubule organizing center • cell body Biological process • protein transport • brain development • lipid metabolism • phototransduction • phosphatidylinositol biosynthetic process • phospholipid transport Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	9600	18739
Ensembl	ENSG00000110697	n/a
UniProt	O00562	O35954
RefSeq (mRNA)	NM_001130848 NM_004910	NM_001136078 NM_008851
RefSeq (protein)	NP_001124320 NP_004901	NP_032877
Location (UCSC)	Chr 11: 67.49 – 67.51 Mb	n/a
PubMed search	[2]	[3]
Wikidata
View/Edit Human View/Edit Mouse

Function

PITPNM1 belongs to a family of proteins that share homology with the Drosophila retinal degeneration B (rdgB) protein.[supplied by OMIM][5]

It was found that aggressive metastasized cancer cells produced more of the PITPNC1 protein. In contrast, tumor cells that had not spread had lower expression of PITPNC1. Studies reveal that PITPNC1 promotes malignant secretion by binding Golgi-resident PI4P and localizing RAB1B to the Golgi. RAB1B localization to the Golgi allows for the recruitment of GOLPH3 (Golgi phosphoprotein 3), which facilitates Golgi extension and enhanced vesicular release. PITPNC1-mediated vesicular release drives metastasis by increasing the secretion of pro-invasive and pro-angiogenic mediators HTRA1, MMP1, FAM3C, PDGFA, and ADAM10.[6]

Interactions

PITPNM1 has been shown to interact with PTK2B.[7]

References

1. GRCh38: Ensembl release 89: ENSG00000110697 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. Rubboli F, Bulfone A, Bogni S, Marchitiello A, Zollo M, Borsani G, Ballabio A, Banfi S (1997). "A mammalian homologue of the Drosophila retinal degeneration B gene: implications for the evolution of phototransduction mechanisms". Genes Funct. 1 (3): 205–13. doi:10.1046/j.1365-4624.1997.00015.x. PMID 9680295.
5. "Entrez Gene: PITPNM1 phosphatidylinositol transfer protein, membrane-associated 1".
6. Halberg N, Sengelaub CA, Navrazhina K, Molina H, Uryu K, Tavazoie SF (2016). "PITPNC1 Recruits RAB1B to the Golgi Network to Drive Malignant Secretion". Cancer Cell. 29 (3): 339–353. doi:10.1016/j.ccell.2016.02.013. PMC 5300038. PMID 26977884.
7. Lev S, Hernandez J, Martinez R, Chen A, Plowman G, Schlessinger J (Mar 1999). "Identification of a novel family of targets of PYK2 related to Drosophila retinal degeneration B (rdgB) protein". Mol. Cell. Biol. 19 (3): 2278–88. doi:10.1128/mcb.19.3.2278. PMC 84020. PMID 10022914.

Further reading

• Vihtelic TS, Hyde DR, O'Tousa JE (1991). "Isolation and characterization of the Drosophila retinal degeneration B (rdgB) gene". Genetics. 127 (4): 761–8. PMC 1204403. PMID 1903119.
• Aikawa Y, Hara H, Watanabe T (1997). "Molecular cloning and characterization of mammalian homologues of the Drosophila retinal degeneration B gene". Biochem. Biophys. Res. Commun. 236 (3): 559–64. doi:10.1006/bbrc.1997.7009. PMID 9245688.
• Tian D, Litvak V, Toledo-Rodriguez M, Carmon S, Lev S (2002). "Nir2, a novel regulator of cell morphogenesis". Mol. Cell. Biol. 22 (8): 2650–62. doi:10.1128/MCB.22.8.2650-2662.2002. PMC 133726. PMID 11909959.
• Litvak V, Tian D, Carmon S, Lev S (2002). "Nir2, a human homolog of Drosophila melanogaster retinal degeneration B protein, is essential for cytokinesis". Mol. Cell. Biol. 22 (14): 5064–75. doi:10.1128/MCB.22.14.5064-5075.2002. PMC 139767. PMID 12077336.
• Litvak V, Shaul YD, Shulewitz M, Amarilio R, Carmon S, Lev S (2002). "Targeting of Nir2 to lipid droplets is regulated by a specific threonine residue within its PI-transfer domain". Curr. Biol. 12 (17): 1513–8. doi:10.1016/S0960-9822(02)01107-7. PMID 12225667.
• Litvak V, Argov R, Dahan N, Ramachandran S, Amarilio R, Shainskaya A, Lev S (2004). "Mitotic phosphorylation of the peripheral Golgi protein Nir2 by Cdk1 provides a docking mechanism for Plk1 and affects cytokinesis completion". Mol. Cell. 14 (3): 319–30. doi:10.1016/S1097-2765(04)00214-X. PMID 15125835.
• Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
• Amarilio R, Ramachandran S, Sabanay H, Lev S (2005). "Differential regulation of endoplasmic reticulum structure through VAP-Nir protein interaction". J. Biol. Chem. 280 (7): 5934–44. doi:10.1074/jbc.M409566200. PMID 15545272.
• Ocaka L, Spalluto C, Wilson DI, Hunt DM, Halford S (2005). "Chromosomal localization, genomic organization and evolution of the genes encoding human phosphatidylinositol transfer protein membrane-associated (PITPNM) 1, 2 and 3". Cytogenet. Genome Res. 108 (4): 293–302. doi:10.1159/000081519. PMID 15627748.
• Litvak V, Dahan N, Ramachandran S, Sabanay H, Lev S (2005). "Maintenance of the diacylglycerol level in the Golgi apparatus by the Nir2 protein is critical for Golgi secretory function". Nat. Cell Biol. 7 (3): 225–34. doi:10.1038/ncb1221. PMID 15723057.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
• Burgis NE, Cunningham RP (2007). "Substrate specificity of RdgB protein, a deoxyribonucleoside triphosphate pyrophosphohydrolase". J. Biol. Chem. 282 (6): 3531–8. doi:10.1074/jbc.M608708200. PMID 17090528.