2efl
Crystal structure of the EFC domain of formin-binding protein 17Crystal structure of the EFC domain of formin-binding protein 17
Template:ABSTRACT PUBMED 17512409
DiseaseDisease
[FNBP1_HUMAN] Note=A chromosomal aberration involving FNBP1 is found in acute leukemias. Translocation t(9;11)(q34;q23) with MLL. The relatively low incidence of the MLL-FNBP1 fusion protein in acute leukemia may reflect the marginal capacity of this fusion protein to induce cellular transformation.
FunctionFunction
[FNBP1_HUMAN] May act as a link between RND2 signaling and regulation of the actin cytoskeleton (By similarity). Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during the late stage of clathrin-mediated endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also enhances actin polymerization via the recruitment of WASL/N-WASP, which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. May be required for the lysosomal retention of FASLG/FASL.[1][2][3][4][5]
About this StructureAbout this Structure
2efl is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Shimada A, Niwa H, Tsujita K, Suetsugu S, Nitta K, Hanawa-Suetsugu K, Akasaka R, Nishino Y, Toyama M, Chen L, Liu ZJ, Wang BC, Yamamoto M, Terada T, Miyazawa A, Tanaka A, Sugano S, Shirouzu M, Nagayama K, Takenawa T, Yokoyama S. Curved EFC/F-BAR-domain dimers are joined end to end into a filament for membrane invagination in endocytosis. Cell. 2007 May 18;129(4):761-72. PMID:17512409 doi:10.1016/j.cell.2007.03.040
- ↑ Kamioka Y, Fukuhara S, Sawa H, Nagashima K, Masuda M, Matsuda M, Mochizuki N. A novel dynamin-associating molecule, formin-binding protein 17, induces tubular membrane invaginations and participates in endocytosis. J Biol Chem. 2004 Sep 17;279(38):40091-9. Epub 2004 Jul 12. PMID:15252009 doi:10.1074/jbc.M404899200
- ↑ Itoh T, Erdmann KS, Roux A, Habermann B, Werner H, De Camilli P. Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins. Dev Cell. 2005 Dec;9(6):791-804. PMID:16326391 doi:10.1016/j.devcel.2005.11.005
- ↑ Qian J, Chen W, Lettau M, Podda G, Zornig M, Kabelitz D, Janssen O. Regulation of FasL expression: a SH3 domain containing protein family involved in the lysosomal association of FasL. Cell Signal. 2006 Aug;18(8):1327-37. Epub 2005 Nov 28. PMID:16318909 doi:10.1016/j.cellsig.2005.10.015
- ↑ Tsujita K, Suetsugu S, Sasaki N, Furutani M, Oikawa T, Takenawa T. Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis. J Cell Biol. 2006 Jan 16;172(2):269-79. PMID:16418535 doi:10.1083/jcb.200508091
- ↑ Shimada A, Niwa H, Tsujita K, Suetsugu S, Nitta K, Hanawa-Suetsugu K, Akasaka R, Nishino Y, Toyama M, Chen L, Liu ZJ, Wang BC, Yamamoto M, Terada T, Miyazawa A, Tanaka A, Sugano S, Shirouzu M, Nagayama K, Takenawa T, Yokoyama S. Curved EFC/F-BAR-domain dimers are joined end to end into a filament for membrane invagination in endocytosis. Cell. 2007 May 18;129(4):761-72. PMID:17512409 doi:10.1016/j.cell.2007.03.040