Profilin 1

Profilin 1
	; PDB rendering based on 1awi.
Available structures
PDB	1AWI, 1CF0, 1CJF, 1FIK, 1FIL, 1PFL, 2PAV, 2PBD, 3CHW
Identifiers
Symbols	PFN1;
External IDs	OMIM: 176610 MGI: 97549 HomoloGene: 3684 GeneCards: PFN1 Gene
Gene Ontology
Molecular function	• actin binding; • receptor binding; • phosphatidylinositol-4,5-bisphosphate binding; • Rho GTPase binding; • proline-rich region binding;
Cellular component	• nucleus; • cytoplasm; • actin cytoskeleton; • synaptosome; • synapse;
Biological process	• neural tube closure; • platelet degranulation; • blood coagulation; • response to organic substance; • actin cytoskeleton organization; • platelet activation; • positive regulation of transcription from RNA polymerase II promoter; • positive regulation of viral transcription; • positive regulation of DNA metabolic process; • positive regulation of stress fiber assembly; • cellular response to growth factor stimulus;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs

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Profilin-1 is a protein that in humans is encoded by the PFN1 gene.^[1]^[2]

The protein encoded by this gene is a ubiquitous actin monomer-binding protein belonging to the profilin family. It is thought to regulate actin polymerization in response to extracellular signals. Deletion of this gene is associated with Miller-Dieker syndrome.^[3]

[edit] Interactions

Profilin 1 has been shown to interact with WASF1,^[4] FMNL1,^[5] WASL,^[6]^[7] MLLT4^[8] and Vasodilator-stimulated phosphoprotein.^[9]

[edit] References

^ Kwiatkowski DJ, Bruns GA (May 1988). "Human profilin. Molecular cloning, sequence comparison, and chromosomal analysis". J Biol Chem 263 (12): 5910–5. PMID 3356709.
^ Kwiatkowski DJ, Aklog L, Ledbetter DH, Morton CC (Apr 1990). "Identification of the functional profilin gene, its localization to chromosome subband 17p13.3, and demonstration of its deletion in some patients with Miller-Dieker syndrome". Am J Hum Genet 46 (3): 559–67. PMC 1683621. PMID 1968707. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1683621.
^ "Entrez Gene: PFN1 profilin 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5216.
^ Miki, H; Suetsugu S, Takenawa T (Dec. 1998). "WAVE, a novel WASP-family protein involved in actin reorganization induced by Rac". EMBO J. (ENGLAND) 17 (23): 6932–41. doi:10.1093/emboj/17.23.6932. ISSN 0261-4189. PMC 1171041. PMID 9843499. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1171041.
^ Yayoshi-Yamamoto, S; Taniuchi I, Watanabe T (Sep. 2000). "FRL, a Novel Formin-Related Protein, Binds to Rac and Regulates Cell Motility and Survival of Macrophages". Mol. Cell. Biol. (UNITED STATES) 20 (18): 6872–81. doi:10.1128/MCB.20.18.6872-6881.2000. ISSN 0270-7306. PMC 86228. PMID 10958683. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=86228.
^ Mimuro, H; Suzuki T, Suetsugu S, Miki H, Takenawa T, Sasakawa C (Sep. 2000). "Profilin is required for sustaining efficient intra- and intercellular spreading of Shigella flexneri". J. Biol. Chem. (UNITED STATES) 275 (37): 28893–901. doi:10.1074/jbc.M003882200. ISSN 0021-9258. PMID 10867004.
^ Suetsugu, S; Miki H, Takenawa T (Nov. 1998). "The essential role of profilin in the assembly of actin for microspike formation". EMBO J. (ENGLAND) 17 (22): 6516–26. doi:10.1093/emboj/17.22.6516. ISSN 0261-4189. PMC 1170999. PMID 9822597. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1170999.
^ Boettner, B; Govek E E, Cross J, Van Aelst L (Aug. 2000). "The junctional multidomain protein AF-6 is a binding partner of the Rap1A GTPase and associates with the actin cytoskeletal regulator profilin". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 97 (16): 9064–9. doi:10.1073/pnas.97.16.9064. ISSN 0027-8424. PMC 16822. PMID 10922060. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=16822.
^ Harbeck, B; Hüttelmaier S, Schluter K, Jockusch B M, Illenberger S (Oct. 2000). "Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin". J. Biol. Chem. (UNITED STATES) 275 (40): 30817–25. doi:10.1074/jbc.M005066200. ISSN 0021-9258. PMID 10882740.

[edit] Further reading

Qualmann B, Kessels MM (2003). "Endocytosis and the cytoskeleton". Int. Rev. Cytol.. International Review of Cytology 220: 93–144. doi:10.1016/S0074-7696(02)20004-2. ISBN 9780123646248. PMID 12224553.
Ampe C, Markey F, Lindberg U, Vandekerckhove J (1988). "The primary structure of human platelet profilin: reinvestigation of the calf spleen profilin sequence". FEBS Lett. 228 (1): 17–21. doi:10.1016/0014-5793(88)80575-1. PMID 3342873.
Gieselmann R, Kwiatkowski DJ, Janmey PA, Witke W (1995). "Distinct biochemical characteristics of the two human profilin isoforms". Eur. J. Biochem. 229 (3): 621–8. doi:10.1111/j.1432-1033.1995.tb20506.x. PMID 7758455.
Kato S, Sekine S, Oh SW, et al. (1995). "Construction of a human full-length cDNA bank". Gene 150 (2): 243–50. doi:10.1016/0378-1119(94)90433-2. PMID 7821789.
Metzler WJ, Constantine KL, Friedrichs MS, et al. (1994). "Characterization of the three-dimensional solution structure of human profilin: 1H, 13C, and 15N NMR assignments and global folding pattern". Biochemistry 32 (50): 13818–29. doi:10.1021/bi00213a010. PMID 8268157.
Schutt CE, Myslik JC, Rozycki MD, et al. (1993). "The structure of crystalline profilin-beta-actin". Nature 365 (6449): 810–6. doi:10.1038/365810a0. PMID 8413665.
Mahoney NM, Janmey PA, Almo SC (1997). "Structure of the profilin-poly-L-proline complex involved in morphogenesis and cytoskeletal regulation". Nat. Struct. Biol. 4 (11): 953–60. doi:10.1038/nsb1197-953. PMID 9360613.
Mammoto A, Sasaki T, Asakura T, et al. (1998). "Interactions of drebrin and gephyrin with profilin". Biochem. Biophys. Res. Commun. 243 (1): 86–9. doi:10.1006/bbrc.1997.8068. PMID 9473484.
Bhargavi V, Chari VB, Singh SS (1998). "Phosphatidylinositol 3-kinase binds to profilin through the p85 alpha subunit and regulates cytoskeletal assembly". Biochem. Mol. Biol. Int. 46 (2): 241–8. PMID 9801792.
Suetsugu S, Miki H, Takenawa T (1999). "The essential role of profilin in the assembly of actin for microspike formation". EMBO J. 17 (22): 6516–26. doi:10.1093/emboj/17.22.6516. PMC 1170999. PMID 9822597. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1170999.
Miki H, Suetsugu S, Takenawa T (1999). "WAVE, a novel WASP-family protein involved in actin reorganization induced by Rac". EMBO J. 17 (23): 6932–41. doi:10.1093/emboj/17.23.6932. PMC 1171041. PMID 9843499. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1171041.
Mahoney NM, Rozwarski DA, Fedorov E, et al. (1999). "Profilin binds proline-rich ligands in two distinct amide backbone orientations". Nat. Struct. Biol. 6 (7): 666–71. doi:10.1038/10722. PMID 10404225.
Nunoi H, Yamazaki T, Tsuchiya H, et al. (1999). "A heterozygous mutation of β-actin associated with neutrophil dysfunction and recurrent infection". Proc. Natl. Acad. Sci. U.S.A. 96 (15): 8693–8. doi:10.1073/pnas.96.15.8693. PMC 17578. PMID 10411937. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=17578.
Murphy GA, Solski PA, Jillian SA, et al. (1999). "Cellular functions of TC10, a Rho family GTPase: regulation of morphology, signal transduction and cell growth". Oncogene 18 (26): 3831–45. doi:10.1038/sj.onc.1202758. PMID 10445846.
Harbeck B, Hüttelmaier S, Schluter K, et al. (2000). "Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin". J. Biol. Chem. 275 (40): 30817–25. doi:10.1074/jbc.M005066200. PMID 10882740.
Boettner B, Govek EE, Cross J, Van Aelst L (2000). "The junctional multidomain protein AF-6 is a binding partner of the Rap1A GTPase and associates with the actin cytoskeletal regulator profilin". Proc. Natl. Acad. Sci. U.S.A. 97 (16): 9064–9. doi:10.1073/pnas.97.16.9064. PMC 16822. PMID 10922060. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=16822.
Yayoshi-Yamamoto S, Taniuchi I, Watanabe T (2000). "FRL, a Novel Formin-Related Protein, Binds to Rac and Regulates Cell Motility and Survival of Macrophages". Mol. Cell. Biol. 20 (18): 6872–81. doi:10.1128/MCB.20.18.6872-6881.2000. PMC 86228. PMID 10958683. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=86228.
Mellon MB, Frank BT, Fang KC (2002). "Mast cell alpha-chymase reduces IgE recognition of birch pollen profilin by cleaving antibody-binding epitopes". J. Immunol. 168 (1): 290–7. PMID 11751973.