Profilin 1

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Profilin 1
Protein PFN1 PDB 1awi.png
PDB rendering based on 1awi.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols PFN1 ; ALS18
External IDs OMIM176610 MGI97549 HomoloGene3684 GeneCards: PFN1 Gene
RNA expression pattern
PBB GE PFN1 200634 at tn.png
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:
4.85 – 4.85 Mb
Chr 11:
70.65 – 70.65 Mb
PubMed search [1] [2]

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]

Interactions[edit]

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

References[edit]

  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. ^ Miki, H; Suetsugu S; Takenawa T (December 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. 
  5. ^ 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. (UNITED STATES) 20 (18): 6872–81. doi:10.1128/MCB.20.18.6872-6881.2000. ISSN 0270-7306. PMC 86228. PMID 10958683. 
  6. ^ 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. (UNITED STATES) 275 (37): 28893–901. doi:10.1074/jbc.M003882200. ISSN 0021-9258. PMID 10867004. 
  7. ^ Suetsugu, S; Miki H; Takenawa T (November 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. 
  8. ^ Boettner, B; Govek E E; 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. (UNITED STATES) 97 (16): 9064–9. doi:10.1073/pnas.97.16.9064. ISSN 0027-8424. PMC 16822. PMID 10922060. 
  9. ^ Harbeck, B; Hüttelmaier S; Schluter K; Jockusch B M; Illenberger S (October 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. 

Further reading[edit]