Profilin 1

Profilin 1
PDB rendering based on 1awi.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1AWI​, 1CF0​, 1CJF​, 1FIK​, 1FIL​, 1PFL​, 2PAV​, 2PBD​, 3CHW​
Identifiers
Symbols	PFN1 ; ALS18
External IDs	OMIM: 176610 MGI: 97549 HomoloGene: 3684 GeneCards: PFN1 Gene
Gene ontology Molecular function • adenyl-nucleotide exchange factor activity • actin binding • actin monomer binding • protein binding • phosphatidylinositol-4,5-bisphosphate binding • Rho GTPase binding • poly(A) RNA binding • proline-rich region binding Cellular component • nucleus • cytoplasm • cytosol • cytoskeleton • focal adhesion • cell cortex • membrane • extracellular exosome • blood microparticle Biological process • neural tube closure • platelet degranulation • regulation of transcription from RNA polymerase II promoter • blood coagulation • positive regulation of epithelial cell migration • actin cytoskeleton organization • platelet activation • negative regulation of actin filament polymerization • positive regulation of actin filament polymerization • negative regulation of actin filament bundle assembly • positive regulation of ATPase activity • protein stabilization • negative regulation of stress fiber assembly • positive regulation of ruffle assembly Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	5216	18643
Ensembl	ENSG00000108518	ENSMUSG00000018293
UniProt	P07737	P62962
RefSeq (mRNA)	NM_005022	NM_011072
RefSeq (protein)	NP_005013	NP_035202
Location (UCSC)	Chr 17: 4.95 – 4.95 Mb	Chr 11: 70.65 – 70.65 Mb
PubMed search

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

Function

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]

Interactions

Profilin 1 has been shown to interact with:

• FMNL1,^[4]
• MLLT4^[5]
• Vasodilator-stimulated phosphoprotein,^[6]
• WASF1,^[7] and
• WASL.^[8][9]

References

1. Kwiatkowski DJ, Bruns GA (May 1988). "Human profilin. Molecular cloning, sequence comparison, and chromosomal analysis". J Biol Chem 263 (12): 5910–5. PMID 3356709.
2. Kwiatkowski DJ, Aklog L, Ledbetter DH, Morton CC (April 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.
3. "Entrez Gene: PFN1 profilin 1".
4. Yayoshi-Yamamoto S, Taniuchi I, Watanabe T (September 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.
5. Boettner B, Govek EE, Cross J, Van Aelst L (August 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.
6. Harbeck B, Hüttelmaier S, Schluter K, Jockusch BM, Illenberger S (October 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.
7. Miki H, Suetsugu S, Takenawa T (December 1998). "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.
8. Mimuro H, Suzuki T, Suetsugu S, Miki H, Takenawa T, Sasakawa C (September 2000). "Profilin is required for sustaining efficient intra- and intercellular spreading of Shigella flexneri". J. Biol. Chem. 275 (37): 28893–901. doi:10.1074/jbc.M003882200. PMID 10867004.
9. Suetsugu S, Miki H, Takenawa T (November 1998). "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.

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 978-0-12-364624-8. 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, Kim NS, Umezawa Y, Abe N, Yokoyama-Kobayashi M, Aoki T (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, Bell AJ, Ernst EG, Lavoie TB, Mueller L (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, Goonesekere NC, Lindberg U (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, Hotta I, Imamura H, Takahashi K, Matsuura Y, Shirao T, Takai Y (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. doi:10.1080/15216549800203752. 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.
• 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.
• Mahoney NM, Rozwarski DA, Fedorov E, Fedorov AA, Almo SC (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, Kato S, Malech HL, Matsuda I, Kanegasaki S (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.
• Murphy GA, Solski PA, Jillian SA, Pérez de la Ossa P, D'Eustachio P, Der CJ, Rush MG (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, Jockusch BM, Illenberger S (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.
• 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.
• 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. doi:10.4049/jimmunol.168.1.290. PMID 11751973.