Phosphoinositide Recognition Domains

作者: Mark A. Lemmon

DOI: 10.1034/J.1600-0854.2004.00071.X

关键词:

摘要: Domains or modules known to bind phosphoinositides have increased dramatically in number over the past few years, and are found proteins involved intracellular trafficking, cellular signaling, cytoskeletal remodeling. Analysis of lipid binding by these domains its structural basis has provided significant insight into mechanism membrane recruitment different phosphoinositides. that target only rare (3-phosphorylated) must with very high affinity, exquisite specificity. This is achieved solely headgroup interactions case certain pleckstrin homology (PH) [which PtdIns(3,4,5)P3 and/or PtdIns(3,4)P2], but requires an additional membrane-insertion oligomerization component PtdIns(3)P-targeting phox (PX) FYVE domains. PtdIns(4,5)P2, which more abundant some 25-fold, do not require same stringent affinity specificity characteristics, tend be diverse structure. The mode phosphoinositide also appears reflect their distinct functions. For example, serve as simple targeting recognize headgroups. By contrast, other domains, notably epsin ENTH domain, appear promote bilayer curvature inserting upon binding.

参考文章(78)
James H. Hurley, Beverly Wendland, Endocytosis: Driving Membranes around the Bend Cell. ,vol. 111, pp. 143- 146 ,(2002) , 10.1016/S0092-8674(02)01044-9
Matthew L. Cheever, Trey K. Sato, Tonny de Beer, Tatiana G. Kutateladze, Scott D. Emr, Michael Overduin, Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes. Nature Cell Biology. ,vol. 3, pp. 613- 618 ,(2001) , 10.1038/35083000
Lucia E. Rameh, Kimberley F. Tolias, Brian C. Duckworth, Lewis C. Cantley, A new pathway for synthesis of phosphatidylinositol-4,5-bisphosphate Nature. ,vol. 390, pp. 192- 196 ,(1997) , 10.1038/36621
Fumihiko Kanai, Hui Liu, Seth J. Field, Hares Akbary, Tsuyoshi Matsuo, Glenn E. Brown, Lewis C. Cantley, Michael B. Yaffe, The PX domains of p47phox and p40phox bind to lipid products of PI(3)K Nature Cell Biology. ,vol. 3, pp. 675- 678 ,(2001) , 10.1038/35083070
Stephen K. Dove, Frank T. Cooke, Michael R. Douglas, Lee G. Sayers, Peter J. Parker, Robert H. Michell, Osmotic stress activates phosphatidylinositol-3,5-bisphosphate synthesis Nature. ,vol. 390, pp. 187- 192 ,(1997) , 10.1038/36613
T Kanematsu, H Takeya, Y Watanabe, S Ozaki, M Yoshida, T Koga, S Iwanaga, M Hirata, Putative Inositol 1,4,5-Trisphosphate Binding Proteins in Rat Brain Cytosol* Journal of Biological Chemistry. ,vol. 267, pp. 6518- 6525 ,(1992) , 10.1016/S0021-9258(19)50458-6
Yue Xu, Heinz Hortsman, Lifong Seet, Siew Heng Wong, Wanjin Hong, SNX3 regulates endosomal function through its PX-domain-mediated interaction with PtdIns(3)P. Nature Cell Biology. ,vol. 3, pp. 658- 666 ,(2001) , 10.1038/35083051
Chris D. Ellson, Stéphanie Gobert-Gosse, Karen E Anderson, Keith Davidson, Hediye Erdjument-Bromage, Paul Tempst, Jan W. Thuring, Matthew A. Cooper, Ze-Yi Lim, Andrew B. Holmes, Piers R. J. Gaffney, John Coadwell, Edwin R. Chilvers, Phill T. Hawkins, Len R. Stephens, PtdIns(3)P regulates the neutrophil oxidase complex by binding to the PX domain of p40(phox). Nature Cell Biology. ,vol. 3, pp. 679- 682 ,(2001) , 10.1038/35083076
M.E. Cifuentes, T. Delaney, M.J. Rebecchi, D-myo-inositol 1,4,5-trisphosphate inhibits binding of phospholipase C-delta 1 to bilayer membranes. Journal of Biological Chemistry. ,vol. 269, pp. 1945- 1948 ,(1994) , 10.1016/S0021-9258(17)42118-1
P. T. Hawkins, L. R. Stephens, S. H. Ridley, P. Lipp, J. W. J. F. Thuring, N. Ktistakis, M. Bootman, H. Erdjument-Bromage, C. D. Ellson, P. Tempst, J. Coadwell, Z.-Y. Lim, M. Manifava, A. Nazarian, M. A. Cooper, A. B. Holmes, K. Davidson, K. E. Anderson, FENS-1 and DFCP1 are FYVE domain-containing proteins with distinct functions in the endosomal and Golgi compartments. Journal of Cell Science. ,vol. 114, pp. 3991- 4000 ,(2001) , 10.1242/JCS.114.22.3991