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Sci. STKE, 16 December 2003
Vol. 2003, Issue 213, p. re16
[DOI: 10.1126/stke.2132003re16]
REVIEWS
Membrane Recognition and Targeting by Lipid-Binding Domains
Jonathan P. DiNitto,
Thomas C. Cronin, and
David G. Lambright*
Program in Molecular Medicine and Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Gloss: With eight figures, one table, and 155 references, this STKE Review describes the structural features that explain how modular domains interact with lipids. Various specific and nonspecific interactions contribute to the ability of proteins to recognize cellular membranes, allowing proteins with lipid-binding domains to play roles in cellular signaling and membrane trafficking.
Phosphoinositides Differentially Regulate Protrudin Localization through the FYVE Domain.
J.-E. Gil, E. Kim, I.-S. Kim, B. Ku, W. S. Park, B.-H. Oh, S. H. Ryu, W. Cho, and W. D. Heo (2012)
J. Biol. Chem.
287, 41268-41276
|Abstract »|Full Text »|PDF »
A structure-based protocol for learning the family-specific mechanisms of membrane-binding domains.
M. Kallberg, N. Bhardwaj, R. Langlois, and H. Lu (2012)
Bioinformatics
28, i431-i437
|Abstract »|Full Text »|PDF »
IQGAP Proteins Reveal an Atypical Phosphoinositide (aPI) Binding Domain with a Pseudo C2 Domain Fold.
M. J. Dixon, A. Gray, M. Schenning, M. Agacan, W. Tempel, Y. Tong, L. Nedyalkova, H.-W. Park, N. R. Leslie, D. M. F. van Aalten, et al. (2012)
J. Biol. Chem.
287, 22483-22496
|Abstract »|Full Text »|PDF »
Structural Basis of Phosphoinositide Binding to Kindlin-2 Protein Pleckstrin Homology Domain in Regulating Integrin Activation.
J. Liu, K. Fukuda, Z. Xu, Y.-Q. Ma, J. Hirbawi, X. Mao, C. Wu, E. F. Plow, and J. Qin (2011)
J. Biol. Chem.
286, 43334-43342
|Abstract »|Full Text »|PDF »
Optical probing of a dynamic membrane interaction that regulates the TREK1 channel.
Structure-Function Study of the N-terminal Domain of Exocyst Subunit Sec3.
K. Baek, A. Knodler, S. H. Lee, X. Zhang, K. Orlando, J. Zhang, T. J. Foskett, W. Guo, and R. Dominguez (2010)
J. Biol. Chem.
285, 10424-10433
|Abstract »|Full Text »|PDF »
Lipid binding domains: more than simple lipid effectors.
Global Topology Analysis of Pancreatic Zymogen Granule Membrane Proteins.
X. Chen, P. J. Ulintz, E. S. Simon, J. A. Williams, and P. C. Andrews (2008)
Mol. Cell. Proteomics
7, 2323-2336
|Abstract »|Full Text »|PDF »
Interaction between the Human Immunodeficiency Virus Type 1 Gag Matrix Domain and Phosphatidylinositol-(4,5)-Bisphosphate Is Essential for Efficient Gag Membrane Binding.
V. Chukkapalli, I. B. Hogue, V. Boyko, W.-S. Hu, and A. Ono (2008)
J. Virol.
82, 2405-2417
|Abstract »|Full Text »|PDF »
The WD40 and FYVE domain containing protein 2 defines a class of early endosomes necessary for endocytosis.
A. Hayakawa, D. Leonard, S. Murphy, S. Hayes, M. Soto, K. Fogarty, C. Standley, K. Bellve, D. Lambright, C. Mello, et al. (2006)
PNAS
103, 11928-11933
|Abstract »|Full Text »|PDF »
Biochemistry. Viral glycoproteins and an evolutionary conundrum..
Ligation of CD28 Stimulates the Formation of a Multimeric Signaling Complex Involving Grb-2-Associated Binder 2 (Gab2), Src Homology Phosphatase-2, and Phosphatidylinositol 3-Kinase: Evidence That Negative Regulation of CD28 Signaling Requires the Gab2 Pleckstrin Homology Domain.
R. V. Parry, G. C. Whittaker, M. Sims, C. E. Edmead, M. J. Welham, and S. G. Ward (2006)
J. Immunol.
176, 594-602
|Abstract »|Full Text »|PDF »
Phosphatidylinositol (4,5) bisphosphate regulates HIV-1 Gag targeting to the plasma membrane.
A. Ono, S. D. Ablan, S. J. Lockett, K. Nagashima, and E. O. Freed (2004)
PNAS
101, 14889-14894
|Abstract »|Full Text »|PDF »
