Association of frabin with specific actin and membrane structures - PubMed (original) (raw)
Association of frabin with specific actin and membrane structures
Yongman Kim et al. Genes Cells. 2002 Apr.
Free article
Abstract
Background: Frabin is an actin filament (F-actin)-binding protein with GDP/GTP exchange activity specific for Cdc42 small G protein. Expression of frabin forms filopodia-like microspikes through the direct activation of Cdc42, and lamellipodia through indirect activation of Rac small G protein. Frabin consists of the F-actin-binding domain (FAB), the Dbl homology domain (DH), the first pleckstrin homology domain (PH1), the FYVE-finger domain (FYVE), the second PH domain (PH2) from the N-terminus in this order. Although DH and PH1 show exchange activity, FAB, in addition to DH and PH1, is required for the formation of microspikes, whereas FYVE and PH2, in addition to DH and PH1, are required for the formation of lamellipodia.
Results: Various truncated mutants of frabin were co-expressed with a dominant active mutant (DA) of Cdc42, Rac1DA, or full-length frabin in L fibroblasts. FAB was recruited to the Cdc42DA-formed filopodia-like microspikes. FAB and a fragment containing DH, PH1, FYVE and PH2 were recruited to the Rac1DA-formed membrane ruffles. Furthermore, each of these fragments served as a dominant negative mutant of frabin when co-expressed with full-length frabin, and inhibited the full-length frabin-formed morphological changes.
Conclusion: These results suggest that frabin recognizes a specific actin structure(s) through FAB and a specific membrane structure(s) through FAB and the region containing DH, PH1, FYVE and PH2. It is likely that frabin associates with the specific actin and membrane structures and activates Cdc42 and Rac in the vicinity of these structures, eventually leading to morphological changes.
Similar articles
- Two actions of frabin: direct activation of Cdc42 and indirect activation of Rac.
Ono Y, Nakanishi H, Nishimura M, Kakizaki M, Takahashi K, Miyahara M, Satoh-Horikawa K, Mandai K, Takai Y. Ono Y, et al. Oncogene. 2000 Jun 22;19(27):3050-8. doi: 10.1038/sj.onc.1203631. Oncogene. 2000. PMID: 10871857 - Cooperation of Cdc42 small G protein-activating and actin filament-binding activities of frabin in microspike formation.
Ikeda W, Nakanishi H, Tanaka Y, Tachibana K, Takai Y. Ikeda W, et al. Oncogene. 2001 Jun 14;20(27):3457-63. doi: 10.1038/sj.onc.1204463. Oncogene. 2001. PMID: 11429692 - Importance of spatial activation of Cdc42 and rac small G proteins by frabin for microspike formation in MDCK cells.
Yasuda T, Ohtsuka T, Inoue E, Yokoyama S, Sakisaka T, Kodama A, Takaishi K, Takai Y. Yasuda T, et al. Genes Cells. 2000 Jul;5(7):583-91. doi: 10.1046/j.1365-2443.2000.00349.x. Genes Cells. 2000. PMID: 10947844 - Frabin and other related Cdc42-specific guanine nucleotide exchange factors couple the actin cytoskeleton with the plasma membrane.
Nakanishi H, Takai Y. Nakanishi H, et al. J Cell Mol Med. 2008 Aug;12(4):1169-76. doi: 10.1111/j.1582-4934.2008.00345.x. Epub 2008 Apr 9. J Cell Mol Med. 2008. PMID: 18410521 Free PMC article. Review. - I-BAR domains, IRSp53 and filopodium formation.
Ahmed S, Goh WI, Bu W. Ahmed S, et al. Semin Cell Dev Biol. 2010 Jun;21(4):350-6. doi: 10.1016/j.semcdb.2009.11.008. Epub 2009 Nov 11. Semin Cell Dev Biol. 2010. PMID: 19913105 Review.
Cited by
- Imbalance of NRG1-ERBB2/3 signalling underlies altered myelination in Charcot-Marie-Tooth disease 4H.
El-Bazzal L, Ghata A, Estève C, Gadacha J, Quintana P, Castro C, Roeckel-Trévisiol N, Lembo F, Lenfant N, Mégarbané A, Borg JP, Lévy N, Bartoli M, Poitelon Y, Roubertoux PL, Delague V, Bernard-Marissal N. El-Bazzal L, et al. Brain. 2023 May 2;146(5):1844-1858. doi: 10.1093/brain/awac402. Brain. 2023. PMID: 36314052 Free PMC article. - EPEC Recruits a Cdc42-Specific GEF, Frabin, To Facilitate PAK Activation and Host Cell Colonization.
Singh V, Hume PJ, Davidson A, Koronakis V. Singh V, et al. mBio. 2020 Nov 3;11(6):e01423-20. doi: 10.1128/mBio.01423-20. mBio. 2020. PMID: 33144373 Free PMC article. - Lowe syndrome-linked endocytic adaptors direct membrane cycling kinetics with OCRL in Dictyostelium discoideum.
Luscher A, Fröhlich F, Barisch C, Littlewood C, Metcalfe J, Leuba F, Palma A, Pirruccello M, Cesareni G, Stagi M, Walther TC, Soldati T, De Camilli P, Swan LE. Luscher A, et al. Mol Biol Cell. 2019 Aug 1;30(17):2268-2282. doi: 10.1091/mbc.E18-08-0510. Epub 2019 Jun 19. Mol Biol Cell. 2019. PMID: 31216233 Free PMC article. - Epstein-Barr virus-encoded LMP1 interacts with FGD4 to activate Cdc42 and thereby promote migration of nasopharyngeal carcinoma cells.
Liu HP, Chen CC, Wu CC, Huang YC, Liu SC, Liang Y, Chang KP, Chang YS. Liu HP, et al. PLoS Pathog. 2012;8(5):e1002690. doi: 10.1371/journal.ppat.1002690. Epub 2012 May 10. PLoS Pathog. 2012. PMID: 22589722 Free PMC article. - Coordination of cytokinesis and cell separation by endosomal targeting of a Cdc42-specific guanine nucleotide exchange factor in Ustilago maydis.
Schink KO, Bölker M. Schink KO, et al. Mol Biol Cell. 2009 Feb;20(3):1081-8. doi: 10.1091/mbc.e08-03-0280. Epub 2008 Dec 10. Mol Biol Cell. 2009. PMID: 19073889 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases
Miscellaneous