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Volumn 303, Issue 5657, 2004, Pages 495-499

BAR Domains as Sensors of Membrane Curvature: The Amphiphysin BAR Structure

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; DIMERIZATION; DIMERS; PROTEINS; YEAST;

EID: 1442317538     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1092586     Document Type: Article
Times cited : (1454)

References (57)
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    • Materials and methods are available as supporting material on Science Online.
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    • We did not see this pan-handle intermediate in our studies of epsin ENTH tubulation (27), which implies that the mechanism of tubulation is different With epsin, we observed an all-or-none tubulation of individual liposomes, whereas amphiphysin initiated a bud and, with higher concentrations, completed the tubule formation.
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    • analytical, ultracentrifugation data (see fig. S1)
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    • note
    • PICK1 has an N-terminal PDZ domain and a C-terminal, BAR domain. The PDZ domain binds and clusters metabotropic glutamate receptors (49) and AMPA receptors (50) and is important in their localization. We could not get good expression of this protein, but we suggest that the BAR domain (white dimerizing the proteins and thus aggregating the receptors) will localize these channels to areas of preferred membrane curvature. ICA69 (islet cell autoantigen of 69 kD) is a diabetes-associated protein related to arfaptin. Although its exact function is unknown, ICA69 is localized to the TGN and is involved in secretion (51, 52).
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    • Both centaurin and oligophrenin bound efficiently to liposomes but tubulated poorly compared with amphiphysin and arfaptin. Thus, higher protein concentrations, 2 to 5 times those of amphiphysin and arfaptin (30 μM in the case of oligophrenin), were required to see tubulation. We did not observe in vivo tubulation with the BAR + PH domain of oligophrenin, but this could be caused by the N-terminal Myc tag.
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    • 2 but does not tubulate them.
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    • Reducing the binding to liposomes was not sufficient to cause BAR proteins to be curvature-sensitive in this assay. Although the mut1 and F9E mutants of amphiphysin 1 bound liposomes more weakly than the wild-type (Fig. 2D), neither showed a curvature preference, Furthermore, the centaurinβ2 BAR and BAR + PH proteins had different binding affinities, yet they had similar curvature sensitivity (Figs. 4B and 5B).
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    • 2 over Ptdlns(4)P or Ptdlns(3)P. Other BAR domains shared this preference for more negatively charged lipids. Full-length arfaptin preferred Ptdlns(4)P, but the lipid specificity seemed to be determined by the N-terminus, which contains a lipid-binding domain (Fig. 3B and B. J. Peter, unpublished data).
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    • note
    • Single-letter abbreviations for the amino acid residues are as follows: A, Ata; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly: H, His; I, Ile; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln: R, Arg; S, Ser; T, Thr, V, Val; W, Trp; and Y, Tyr.
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    • note
    • We thank the Kazusa DNA Research Institute, the I.M.A.G.E. consortium, S. Gamblin, and M. Lazdunski for sharing plasmids; A. Thompson for help at the ESRF; and G. Praefcke for purified Dab2, I.G.M. was supported by an MRC postdoctoral fellowship, and B.J.P. was supported by an EMBO long-term postdoctoral fellowship.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.