Profilin 1

From Wikipedia, the free encyclopedia

Profilin 1

PDB rendering based on 1awi.

Available structures: 1awi, 1cf0, 1cjf, 1fik, 1fil, 1hlu, 1pfl, 1pne, 2btf

Identifiers

Symbol(s)

PFN1;

External IDs

OMIM: 176610 MGI: 97549 HomoloGene: 3684

Gene ontology
Molecular Function:	• actin monomer binding • protein binding
Cellular Component:	• nucleus • cytoplasm • actin cytoskeleton
Biological Process:	• neural tube closure • regulation of transcription from RNA polymerase II promoter • cytoskeleton organization and biogenesis • actin cytoskeleton organization and biogenesis

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_005022 (mRNA)
NP_005013 (protein)

NM_011072 (mRNA)
NP_035202 (protein)

Location

Chr 17: 4.79 - 4.79 Mb

n/a

Pubmed search

[1]

[2]

Profilin 1, also known as PFN1, is a human gene.

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.^[1]

[edit] References

^ Entrez Gene: PFN1 profilin 1.

[edit] Further reading

Qualmann B, Kessels MM (2003). "Endocytosis and the cytoskeleton.". Int. Rev. Cytol. 220: 93–144. PMID 12224553.
Kwiatkowski DJ, Aklog L, Ledbetter DH, Morton CC (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. PMID 1968707.
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. PMID 3342873.
Kwiatkowski DJ, Bruns GA (1988). "Human profilin. Molecular cloning, sequence comparison, and chromosomal analysis.". J. Biol. Chem. 263 (12): 5910–5. PMID 3356709.
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. PMID 7758455.
Kato S, Sekine S, Oh SW, et al. (1995). "Construction of a human full-length cDNA bank.". Gene 150 (2): 243–50. 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. 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. 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. 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. PMID 9843499.
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 beta-actin associated with neutrophil dysfunction and recurrent infection.". Proc. Natl. Acad. Sci. U.S.A. 96 (15): 8693–8. PMID 10411937.
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. 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. 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. PMID 11751973.