PACSIN1, F-BAR
Short name | PACSIN1_F-BAR |
Overlapping homologous superfamilies | |
domain relationships |
Description
References
1.Molecular mechanism of membrane constriction and tubulation mediated by the F-BAR protein Pacsin/Syndapin. Wang Q, Navarro MV, Peng G, Molinelli E, Shih LG, Judson BL, Rajashankar KR, Sondermann H. Proc. Natl. Acad. Sci. U.S.A. (2009). PMID: 19549836
2.F-BAR proteins of the syndapin family shape the plasma membrane and are crucial for neuromorphogenesis. Dharmalingam E, Haeckel A, Pinyol R, Schwintzer L, Koch D, Kessels MM, Qualmann B. J. Neurosci. 29, 13315-27, (2009). View articlePMID: 19846719
3.PACSIN, a brain protein that is upregulated upon differentiation into neuronal cells. Plomann M, Lange R, Vopper G, Cremer H, Heinlein UA, Scheff S, Baldwin SA, Leitges M, Cramer M, Paulsson M, Barthels D. Eur. J. Biochem. 256, 201-11, (1998). View articlePMID: 9746365
4.Versatile membrane deformation potential of activated pacsin. Goh SL, Wang Q, Byrnes LJ, Sondermann H. PLoS ONE 7, e51628, (2012). View articlePMID: 23236520
5.PACSIN 3 is a novel SH3 domain cytoplasmic adapter protein of the pacsin-syndapin-FAP52 gene family. Sumoy L, Pluvinet R, Andreu N, Estivill X, Escarceller M. Gene 262, 199-205, (2001). View articlePMID: 11179684
6.Phosphorylation of syndapin I F-BAR domain at two helix-capping motifs regulates membrane tubulation. Quan A, Xue J, Wielens J, Smillie KJ, Anggono V, Parker MW, Cousin MA, Graham ME, Robinson PJ. Proc. Natl. Acad. Sci. U.S.A. 109, 3760-5, (2012). View articlePMID: 22355135
GO terms
biological process
molecular function
- None
cellular component
- None
Contributing Member Database Entry
- CDD:cd07680