-
1
-
-
0041765833
-
Mechanisms of membrane deformation
-
Farsad K., and De Camilli P. Mechanisms of membrane deformation. Curr Opin Cell Biol 15 (2003) 372-381
-
(2003)
Curr Opin Cell Biol
, vol.15
, pp. 372-381
-
-
Farsad, K.1
De Camilli, P.2
-
2
-
-
28444476999
-
Membrane curvature and mechanisms of dynamic cell membrane remodelling
-
McMahon H.T., and Gallop J.L. Membrane curvature and mechanisms of dynamic cell membrane remodelling. Nature 438 (2005) 590-596
-
(2005)
Nature
, vol.438
, pp. 590-596
-
-
McMahon, H.T.1
Gallop, J.L.2
-
3
-
-
33644846421
-
How proteins produce cellular membrane curvature
-
Zimmerberg J., and Kozlov M.M. How proteins produce cellular membrane curvature. Nat Rev Mol Cell Biol 7 (2006) 9-19
-
(2006)
Nat Rev Mol Cell Biol
, vol.7
, pp. 9-19
-
-
Zimmerberg, J.1
Kozlov, M.M.2
-
4
-
-
23944488301
-
Sar1p N-terminal helix initiates membrane curvature and completes the fission of a COPII vesicle
-
•]) show that the adsorption of the N-terminal helix of Sar1 to artificial liposomes induces membrane curvature through the penetration of hydrophobic residues and contributes to the overall remodeling of the membrane by the entire COPII coat. Surprisingly, the N-terminal helix of Sar1 is important not only for the initial steps of membrane deformation but also for fission. The two studies disagree on the role of GTP hydrolysis at this point.
-
•]) show that the adsorption of the N-terminal helix of Sar1 to artificial liposomes induces membrane curvature through the penetration of hydrophobic residues and contributes to the overall remodeling of the membrane by the entire COPII coat. Surprisingly, the N-terminal helix of Sar1 is important not only for the initial steps of membrane deformation but also for fission. The two studies disagree on the role of GTP hydrolysis at this point.
-
(2005)
Cell
, vol.122
, pp. 605-617
-
-
Lee, M.C.1
Orci, L.2
Hamamoto, S.3
Futai, E.4
Ravazzola, M.5
Schekman, R.6
-
6
-
-
0037136560
-
Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat
-
Bi X., Corpina R.A., and Goldberg J. Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat. Nature 419 (2002) 271-277
-
(2002)
Nature
, vol.419
, pp. 271-277
-
-
Bi, X.1
Corpina, R.A.2
Goldberg, J.3
-
7
-
-
30544436808
-
Structure of the Sec13/31 COPII coat cage
-
How does Sec13/3 self-assemble and impose the spherical structure of the COPII coat? This cryoEM study gives the answer by establishing the geometry of a minimal Sec13/31 cage. The lattice is different from that of clathrin as it is made from elementary triangles and squares instead of pentagons and hexagons and does not involve extensive interdigitations between proteins.
-
Stagg S.M., Gurkan C., Fowler D.M., LaPointe P., Foss T.R., Potter C.S., Carragher B., and Balch W.E. Structure of the Sec13/31 COPII coat cage. Nature 439 (2006) 234-238. How does Sec13/3 self-assemble and impose the spherical structure of the COPII coat? This cryoEM study gives the answer by establishing the geometry of a minimal Sec13/31 cage. The lattice is different from that of clathrin as it is made from elementary triangles and squares instead of pentagons and hexagons and does not involve extensive interdigitations between proteins.
-
(2006)
Nature
, vol.439
, pp. 234-238
-
-
Stagg, S.M.1
Gurkan, C.2
Fowler, D.M.3
LaPointe, P.4
Foss, T.R.5
Potter, C.S.6
Carragher, B.7
Balch, W.E.8
-
8
-
-
0036866606
-
Arf, Arl, Arp and Sar proteins: a family of GTP-binding proteins with a structural device for 'front-back' communication
-
Pasqualato S., Renault L., and Cherfils J. Arf, Arl, Arp and Sar proteins: a family of GTP-binding proteins with a structural device for 'front-back' communication. EMBO Rep 3 (2002) 1035-1041
-
(2002)
EMBO Rep
, vol.3
, pp. 1035-1041
-
-
Pasqualato, S.1
Renault, L.2
Cherfils, J.3
-
9
-
-
0001718634
-
Biological membranes as bilayer couples. A molecular mechanism of drug-erythrocyte interactions
-
Sheetz M.P., and Singer S.J. Biological membranes as bilayer couples. A molecular mechanism of drug-erythrocyte interactions. Proc Natl Acad Sci USA 71 (1974) 4457-4461
-
(1974)
Proc Natl Acad Sci USA
, vol.71
, pp. 4457-4461
-
-
Sheetz, M.P.1
Singer, S.J.2
-
10
-
-
27644582902
-
Cell biology: helices sculpt membrane
-
Drin G., and Antonny B. Cell biology: helices sculpt membrane. Nature 437 (2005) 1247-1249
-
(2005)
Nature
, vol.437
, pp. 1247-1249
-
-
Drin, G.1
Antonny, B.2
-
11
-
-
0034965355
-
Dynamics of the COPII coat with GTP and stable analogues
-
Antonny B., Madden D., Hamamoto S., Orci L., and Schekman R. Dynamics of the COPII coat with GTP and stable analogues. Nat Cell Biol 3 (2001) 531-537
-
(2001)
Nat Cell Biol
, vol.3
, pp. 531-537
-
-
Antonny, B.1
Madden, D.2
Hamamoto, S.3
Orci, L.4
Schekman, R.5
-
12
-
-
0035423555
-
ER export: public transportation by the COPII coach
-
Antonny B., and Schekman R. ER export: public transportation by the COPII coach. Curr Opin Cell Biol 13 (2001) 438-443
-
(2001)
Curr Opin Cell Biol
, vol.13
, pp. 438-443
-
-
Antonny, B.1
Schekman, R.2
-
13
-
-
9144229521
-
GTP/GDP exchange by Sec12p enables COPII vesicle bud formation on synthetic liposomes
-
Futai E., Hamamoto S., Orci L., and Schekman R. GTP/GDP exchange by Sec12p enables COPII vesicle bud formation on synthetic liposomes. Embo J 23 (2004) 4146-4155
-
(2004)
Embo J
, vol.23
, pp. 4146-4155
-
-
Futai, E.1
Hamamoto, S.2
Orci, L.3
Schekman, R.4
-
14
-
-
30944466040
-
Secretory cargo regulates the turnover of COPII subunits at single ER exit sites
-
Forster R., Weiss M., Zimmermann T., Reynaud E.G., Verissimo F., Stephens D.J., and Pepperkok R. Secretory cargo regulates the turnover of COPII subunits at single ER exit sites. Curr Biol 16 (2006) 173-179
-
(2006)
Curr Biol
, vol.16
, pp. 173-179
-
-
Forster, R.1
Weiss, M.2
Zimmermann, T.3
Reynaud, E.G.4
Verissimo, F.5
Stephens, D.J.6
Pepperkok, R.7
-
15
-
-
0019813567
-
Assembly and packing of clathrin into coats
-
Crowther R.A., and Pearse B.M. Assembly and packing of clathrin into coats. J Cell Biol 91 (1981) 790-797
-
(1981)
J Cell Biol
, vol.91
, pp. 790-797
-
-
Crowther, R.A.1
Pearse, B.M.2
-
16
-
-
10344262047
-
Molecular model for a complete clathrin lattice from electron cryomicroscopy
-
This paper describes the structure of the clathrin coat at subnanometer resolution.
-
Fotin A., Cheng Y., Sliz P., Grigorieff N., Harrison S.C., Kirchhausen T., and Walz T. Molecular model for a complete clathrin lattice from electron cryomicroscopy. Nature 432 (2004) 573-579. This paper describes the structure of the clathrin coat at subnanometer resolution.
-
(2004)
Nature
, vol.432
, pp. 573-579
-
-
Fotin, A.1
Cheng, Y.2
Sliz, P.3
Grigorieff, N.4
Harrison, S.C.5
Kirchhausen, T.6
Walz, T.7
-
17
-
-
0035889088
-
Generation of high curvature membranes mediated by direct endophilin bilayer interactions
-
Farsad K., Ringstad N., Takei K., Floyd S.R., Rose K., and De Camilli P. Generation of high curvature membranes mediated by direct endophilin bilayer interactions. J Cell Biol 155 (2001) 193-200
-
(2001)
J Cell Biol
, vol.155
, pp. 193-200
-
-
Farsad, K.1
Ringstad, N.2
Takei, K.3
Floyd, S.R.4
Rose, K.5
De Camilli, P.6
-
18
-
-
22744442219
-
ArfGAP1 responds to membrane curvature through the folding of a lipid packing sensor motif
-
A central region of ∼30 amino acids of ArfGAP1 is shown to be responsible for the hypersensitivity of ArfGAP1 to membrane curvature. This ALPS motif (ArfGAP1 lipid-packing sensor) is unfolded in solution but adopts an α-helical conformation on highly curved liposomes. Interestingly the polar face of the helix consists almost exclusively of serine and threonine residues. This original feature probably explains the preference of ArfGAP1 for membranes with packing defects.
-
Bigay J., Casella J.F., Drin G., Mesmin B., and Antonny B. ArfGAP1 responds to membrane curvature through the folding of a lipid packing sensor motif. Embo J 24 (2005) 2244-2253. A central region of ∼30 amino acids of ArfGAP1 is shown to be responsible for the hypersensitivity of ArfGAP1 to membrane curvature. This ALPS motif (ArfGAP1 lipid-packing sensor) is unfolded in solution but adopts an α-helical conformation on highly curved liposomes. Interestingly the polar face of the helix consists almost exclusively of serine and threonine residues. This original feature probably explains the preference of ArfGAP1 for membranes with packing defects.
-
(2005)
Embo J
, vol.24
, pp. 2244-2253
-
-
Bigay, J.1
Casella, J.F.2
Drin, G.3
Mesmin, B.4
Antonny, B.5
-
19
-
-
33645240463
-
Golgi localization determinants in ArfGAP1 and in new tissue-specific ArfGAP1 isoforms
-
Parnis A., Rawet M., Regev L., Barkan B., Rotman M., Gaitner M., and Cassel D. Golgi localization determinants in ArfGAP1 and in new tissue-specific ArfGAP1 isoforms. J Biol Chem 281 (2006) 3785-3792
-
(2006)
J Biol Chem
, vol.281
, pp. 3785-3792
-
-
Parnis, A.1
Rawet, M.2
Regev, L.3
Barkan, B.4
Rotman, M.5
Gaitner, M.6
Cassel, D.7
-
20
-
-
0027892019
-
Cholesterol and the Golgi apparatus
-
Bretscher M.S., and Munro S. Cholesterol and the Golgi apparatus. Science 261 (1993) 1280-1281
-
(1993)
Science
, vol.261
, pp. 1280-1281
-
-
Bretscher, M.S.1
Munro, S.2
-
21
-
-
14644393694
-
Lipid traffic: floppy drives and a superhighway
-
Holthuis J.C., and Levine T.P. Lipid traffic: floppy drives and a superhighway. Nat Rev Mol Cell Biol 6 (2005) 209-220
-
(2005)
Nat Rev Mol Cell Biol
, vol.6
, pp. 209-220
-
-
Holthuis, J.C.1
Levine, T.P.2
-
22
-
-
0346756190
-
Lipid packing sensed by ArfGAP1 couples COPI coat disassembly to membrane bilayer curvature
-
Bigay J., Gounon P., Robineau S., and Antonny B. Lipid packing sensed by ArfGAP1 couples COPI coat disassembly to membrane bilayer curvature. Nature 426 (2003) 563-566
-
(2003)
Nature
, vol.426
, pp. 563-566
-
-
Bigay, J.1
Gounon, P.2
Robineau, S.3
Antonny, B.4
-
23
-
-
1442317538
-
BAR domains as sensors of membrane curvature: the amphiphysin BAR structure
-
Using a combination of X-ray crystallography, biochemical assays on liposomes of various size and cellular studies, this study establishes the structural and functional basis for the recognition of membrane curvature by the BAR domain. This domain is an elongated dimer made up of long coiled-coil helices. The overall shape looks like a banana with a concave face decorated with basic residues. Through this face, the BAR domain interacts preferentially with negatively charged and highly curved membranes. With additional domains or motifs, proteins with a BAR domain can detect simultaneously the curvature and lipid composition of a given membrane or can induce membrane curvature.
-
Peter B.J., Kent H.M., Mills I.G., Vallis Y., Butler P.J., Evans P.R., and McMahon H.T. BAR domains as sensors of membrane curvature: the amphiphysin BAR structure. Science 303 (2004) 495-499. Using a combination of X-ray crystallography, biochemical assays on liposomes of various size and cellular studies, this study establishes the structural and functional basis for the recognition of membrane curvature by the BAR domain. This domain is an elongated dimer made up of long coiled-coil helices. The overall shape looks like a banana with a concave face decorated with basic residues. Through this face, the BAR domain interacts preferentially with negatively charged and highly curved membranes. With additional domains or motifs, proteins with a BAR domain can detect simultaneously the curvature and lipid composition of a given membrane or can induce membrane curvature.
-
(2004)
Science
, vol.303
, pp. 495-499
-
-
Peter, B.J.1
Kent, H.M.2
Mills, I.G.3
Vallis, Y.4
Butler, P.J.5
Evans, P.R.6
McMahon, H.T.7
-
24
-
-
28444452974
-
Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins
-
•] present a new branch of the BAR domain family. In addition, interesting observations are made on the combined effects of BAR domains, dynamin and the actin cytoskeleton on membrane deformation and fission. A membrane that is made elastic by a lack of adhesion to the actin cytoskeleton is more readily deformed by BAR domains into long tubules, but less prone to membrane fission by dynamin. This suggests that the membrane-cytoskeleton adhesion must be kept within an optimal range to permit both invagination and fission.
-
•] present a new branch of the BAR domain family. In addition, interesting observations are made on the combined effects of BAR domains, dynamin and the actin cytoskeleton on membrane deformation and fission. A membrane that is made elastic by a lack of adhesion to the actin cytoskeleton is more readily deformed by BAR domains into long tubules, but less prone to membrane fission by dynamin. This suggests that the membrane-cytoskeleton adhesion must be kept within an optimal range to permit both invagination and fission.
-
(2005)
Dev Cell
, vol.9
, pp. 791-804
-
-
Itoh, T.1
Erdmann, K.S.2
Roux, A.3
Habermann, B.4
Werner, H.5
De Camilli, P.6
-
26
-
-
18444366155
-
Role of curvature and phase transition in lipid sorting and fission of membrane tubules
-
When molecular motors walking on microtubules pull the membrane of giant liposomes, they trigger the formation of long and thin tubules, which can be observed by optical microscopy. Their diameter (in the range of tens of nanometers) reflects a compromise between membrane tension (due to the membrane area consumed by the tubule) and membrane bending rigidity. This system is used to assess the bending rigidity of liquid-disordered and liquid-ordered lipid phases and to study the effect of membrane curvature on lipid sorting. Moreover, phase separation in a pulled tubule triggers fission, suggesting an elegant mechanism by which fission could be coupled to lipid sorting and membrane curvature.
-
Roux A., Cuvelier D., Nassoy P., Prost J., Bassereau P., and Goud B. Role of curvature and phase transition in lipid sorting and fission of membrane tubules. Embo J 24 (2005) 1537-1545. When molecular motors walking on microtubules pull the membrane of giant liposomes, they trigger the formation of long and thin tubules, which can be observed by optical microscopy. Their diameter (in the range of tens of nanometers) reflects a compromise between membrane tension (due to the membrane area consumed by the tubule) and membrane bending rigidity. This system is used to assess the bending rigidity of liquid-disordered and liquid-ordered lipid phases and to study the effect of membrane curvature on lipid sorting. Moreover, phase separation in a pulled tubule triggers fission, suggesting an elegant mechanism by which fission could be coupled to lipid sorting and membrane curvature.
-
(2005)
Embo J
, vol.24
, pp. 1537-1545
-
-
Roux, A.1
Cuvelier, D.2
Nassoy, P.3
Prost, J.4
Bassereau, P.5
Goud, B.6
-
28
-
-
0034255144
-
Modulation of CTP:phosphocholine cytidylyltransferase by membrane curvature elastic stress
-
Attard G.S., Templer R.H., Smith W.S., Hunt A.N., and Jackowski S. Modulation of CTP:phosphocholine cytidylyltransferase by membrane curvature elastic stress. Proc Natl Acad Sci U S A 97 (2000) 9032-9036
-
(2000)
Proc Natl Acad Sci U S A
, vol.97
, pp. 9032-9036
-
-
Attard, G.S.1
Templer, R.H.2
Smith, W.S.3
Hunt, A.N.4
Jackowski, S.5
-
29
-
-
7044232102
-
Nonbilayer lipids affect peripheral and integral membrane proteins via changes in the lateral pressure profile
-
Despite the fact that conical lipids have a preference for non-bilayer structures, they are present in biological lipid bilayers. This review explains the advantage of this counterintuitive feature and details the concepts of lipid packing defects and curvature stress, in other words the 'frustration' created by having two back-to-back monolayers with opposite tendencies to curve. These concepts are key for understanding the behavior of peripheral proteins such as ArfGAP1 and CTP:Phosphocholine Cytidylyltransferase.
-
van den Brink-van der Laan E., Killian J.A., and de Kruijff B. Nonbilayer lipids affect peripheral and integral membrane proteins via changes in the lateral pressure profile. Biochim Biophys Acta 1666 (2004) 275-288. Despite the fact that conical lipids have a preference for non-bilayer structures, they are present in biological lipid bilayers. This review explains the advantage of this counterintuitive feature and details the concepts of lipid packing defects and curvature stress, in other words the 'frustration' created by having two back-to-back monolayers with opposite tendencies to curve. These concepts are key for understanding the behavior of peripheral proteins such as ArfGAP1 and CTP:Phosphocholine Cytidylyltransferase.
-
(2004)
Biochim Biophys Acta
, vol.1666
, pp. 275-288
-
-
van den Brink-van der Laan, E.1
Killian, J.A.2
de Kruijff, B.3
-
30
-
-
0036329207
-
Activity of specific lipid-regulated ADP ribosylation factor-GTPase-activating proteins is required for Sec14p-dependent Golgi secretory function in yeast
-
Yanagisawa L.L., Marchena J., Xie Z., Li X., Poon P.P., Singer R.A., Johnston G.C., Randazzo P.A., and Bankaitis V.A. Activity of specific lipid-regulated ADP ribosylation factor-GTPase-activating proteins is required for Sec14p-dependent Golgi secretory function in yeast. Mol Biol Cell 13 (2002) 2193-2206
-
(2002)
Mol Biol Cell
, vol.13
, pp. 2193-2206
-
-
Yanagisawa, L.L.1
Marchena, J.2
Xie, Z.3
Li, X.4
Poon, P.P.5
Singer, R.A.6
Johnston, G.C.7
Randazzo, P.A.8
Bankaitis, V.A.9
-
31
-
-
24644457550
-
Membrane metabolism mediated by Sec14 family members influences Arf GTPase activating protein activity for transport from the trans-Golgi
-
Wong T.A., Fairn G.D., Poon P.P., Shmulevitz M., McMaster C.R., Singer R.A., and Johnston G.C. Membrane metabolism mediated by Sec14 family members influences Arf GTPase activating protein activity for transport from the trans-Golgi. Proc Natl Acad Sci U S A 102 (2005) 12777-12782
-
(2005)
Proc Natl Acad Sci U S A
, vol.102
, pp. 12777-12782
-
-
Wong, T.A.1
Fairn, G.D.2
Poon, P.P.3
Shmulevitz, M.4
McMaster, C.R.5
Singer, R.A.6
Johnston, G.C.7
-
32
-
-
31944436780
-
Depletion of phosphatidylcholine in yeast induces shortening and increased saturation of the lipid acyl chains: evidence for regulation of intrinsic membrane curvature in a eukaryote
-
Yeast synthesizes the major lipid phosphatidylcholine by two metabolic pathways. Surprisingly, a yeast strain deficient in one of these pathways and that cannot use the second pathway, because of the lack of choline in the medium, can grow for 4-5 generations. The amount of phosphatidylcholine decreases from 40% to 2% and this is compensated in part by an increase in phosphatidylethanolamine. Importantly, this substitution is accompanied by acyl chain remodeling. The acyl chains of phosphatidylethanolamine become smaller and more saturated, such as to make this lipid a kind of scale model of phosphatidylcholine. This suggests that the cell adjusts the geometry of lipids to keep the packing (or curvature stress) in membranes within an optimal range.
-
Boumann H.A., Gubbens J., Koorengevel M.C., Oh C.S., Martin C.E., Heck A.J., Patton-Vogt J., Henry S.A., de Kruijff B., and de Kroon A.I. Depletion of phosphatidylcholine in yeast induces shortening and increased saturation of the lipid acyl chains: evidence for regulation of intrinsic membrane curvature in a eukaryote. Mol Biol Cell 17 (2006) 1006-1017. Yeast synthesizes the major lipid phosphatidylcholine by two metabolic pathways. Surprisingly, a yeast strain deficient in one of these pathways and that cannot use the second pathway, because of the lack of choline in the medium, can grow for 4-5 generations. The amount of phosphatidylcholine decreases from 40% to 2% and this is compensated in part by an increase in phosphatidylethanolamine. Importantly, this substitution is accompanied by acyl chain remodeling. The acyl chains of phosphatidylethanolamine become smaller and more saturated, such as to make this lipid a kind of scale model of phosphatidylcholine. This suggests that the cell adjusts the geometry of lipids to keep the packing (or curvature stress) in membranes within an optimal range.
-
(2006)
Mol Biol Cell
, vol.17
, pp. 1006-1017
-
-
Boumann, H.A.1
Gubbens, J.2
Koorengevel, M.C.3
Oh, C.S.4
Martin, C.E.5
Heck, A.J.6
Patton-Vogt, J.7
Henry, S.A.8
de Kruijff, B.9
de Kroon, A.I.10
-
33
-
-
28444437745
-
Endophilin and CtBP/BARS are not acyl transferases in endocytosis or Golgi fission
-
Endophilin and CtBP/BARS have been proposed to contribute to negative curvature at the neck of membrane buds through an acyl-transferase activity. This paper shows that this is a purification artefact.
-
Gallop J.L., Butler P.J., and McMahon H.T. Endophilin and CtBP/BARS are not acyl transferases in endocytosis or Golgi fission. Nature 438 (2005) 675-678. Endophilin and CtBP/BARS have been proposed to contribute to negative curvature at the neck of membrane buds through an acyl-transferase activity. This paper shows that this is a purification artefact.
-
(2005)
Nature
, vol.438
, pp. 675-678
-
-
Gallop, J.L.1
Butler, P.J.2
McMahon, H.T.3
-
34
-
-
28844456020
-
Equivalent effects of snake PLA2 neurotoxins and lysophospholipid-fatty acid mixtures
-
Rigoni M., Caccin P., Gschmeissner S., Koster G., Postle A.D., Rossetto O., Schiavo G., and Montecucco C. Equivalent effects of snake PLA2 neurotoxins and lysophospholipid-fatty acid mixtures. Science 310 (2005) 1678-1680
-
(2005)
Science
, vol.310
, pp. 1678-1680
-
-
Rigoni, M.1
Caccin, P.2
Gschmeissner, S.3
Koster, G.4
Postle, A.D.5
Rossetto, O.6
Schiavo, G.7
Montecucco, C.8
-
35
-
-
0037078331
-
ARFGAP1 promotes the formation of COPI vesicles, suggesting function as a component of the coat
-
Yang J.S., Lee S.Y., Gao M., Bourgoin S., Randazzo P.A., Premont R.T., and Hsu V.W. ARFGAP1 promotes the formation of COPI vesicles, suggesting function as a component of the coat. J Cell Biol 159 (2002) 69-78
-
(2002)
J Cell Biol
, vol.159
, pp. 69-78
-
-
Yang, J.S.1
Lee, S.Y.2
Gao, M.3
Bourgoin, S.4
Randazzo, P.A.5
Premont, R.T.6
Hsu, V.W.7
-
36
-
-
4344586301
-
Rapid constriction of lipid bilayers by the mechanochemical enzyme dynamin
-
This study re-evaluates the mechanical properties of dynamin on liposomes by two different electron microscopy techniques (cryo-EM and negative staining on carbon-coated grids). The two techniques show that dynamin spirals constrict upon GTP hydrolysis. Yet this constriction drives fission only if the lipid membrane lies on the EM grid. This suggests that the mechanical stress imposed by dynamin must be coupled to the anchorage of the bilayer in order to promote fission.
-
Danino D., Moon K.H., and Hinshaw J.E. Rapid constriction of lipid bilayers by the mechanochemical enzyme dynamin. J Struct Biol 147 (2004) 259-267. This study re-evaluates the mechanical properties of dynamin on liposomes by two different electron microscopy techniques (cryo-EM and negative staining on carbon-coated grids). The two techniques show that dynamin spirals constrict upon GTP hydrolysis. Yet this constriction drives fission only if the lipid membrane lies on the EM grid. This suggests that the mechanical stress imposed by dynamin must be coupled to the anchorage of the bilayer in order to promote fission.
-
(2004)
J Struct Biol
, vol.147
, pp. 259-267
-
-
Danino, D.1
Moon, K.H.2
Hinshaw, J.E.3
-
37
-
-
0035344650
-
Cell control by membrane-cytoskeleton adhesion
-
Sheetz M.P. Cell control by membrane-cytoskeleton adhesion. Nat Rev Mol Cell Biol 2 (2001) 392-396
-
(2001)
Nat Rev Mol Cell Biol
, vol.2
, pp. 392-396
-
-
Sheetz, M.P.1
-
38
-
-
0034139820
-
Actin assembly plays a variable, but not obligatory role in receptor-mediated endocytosis in mammalian cells
-
Fujimoto L.M., Roth R., Heuser J.E., and Schmid S.L. Actin assembly plays a variable, but not obligatory role in receptor-mediated endocytosis in mammalian cells. Traffic 1 (2000) 161-171
-
(2000)
Traffic
, vol.1
, pp. 161-171
-
-
Fujimoto, L.M.1
Roth, R.2
Heuser, J.E.3
Schmid, S.L.4
-
39
-
-
26844517614
-
A modular design for the clathrin- and actin-mediated endocytosis machinery
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Live cell imaging is combined with genetics to uncover the mechanisms of endocytosis in yeast. This terrific study identifies four protein modules that act sequentially to produce vesicles and illuminates how coat proteins and the actin cytoskeleton can cooperate in such a process.
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Kaksonen M., Toret C.P., and Drubin D.G. A modular design for the clathrin- and actin-mediated endocytosis machinery. Cell 123 (2005) 305-320. Live cell imaging is combined with genetics to uncover the mechanisms of endocytosis in yeast. This terrific study identifies four protein modules that act sequentially to produce vesicles and illuminates how coat proteins and the actin cytoskeleton can cooperate in such a process.
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(2005)
Cell
, vol.123
, pp. 305-320
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Kaksonen, M.1
Toret, C.P.2
Drubin, D.G.3
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40
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Coupling between clathrin-coated-pit invagination, cortactin recruitment, and membrane scission observed in live cells
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By combining evanescent field and epi fluorescence microscopy, one can follow the inward movement of clathrin-coated structures from the plasma membrane. Whether this movement corresponds simply to membrane invagination or also includes fission is not clear. To resolve this, an optical technique based on the accessibility of a cargo molecule to extracellular protons is presented, which permits the detection of single membrane fission events. Fission is shown to correlate with a peak recruitment of cortactin, which is a dynamin- and actin-binding protein.
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Merrifield C.J., Perrais D., and Zenisek D. Coupling between clathrin-coated-pit invagination, cortactin recruitment, and membrane scission observed in live cells. Cell 121 (2005) 593-606. By combining evanescent field and epi fluorescence microscopy, one can follow the inward movement of clathrin-coated structures from the plasma membrane. Whether this movement corresponds simply to membrane invagination or also includes fission is not clear. To resolve this, an optical technique based on the accessibility of a cargo molecule to extracellular protons is presented, which permits the detection of single membrane fission events. Fission is shown to correlate with a peak recruitment of cortactin, which is a dynamin- and actin-binding protein.
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(2005)
Cell
, vol.121
, pp. 593-606
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Merrifield, C.J.1
Perrais, D.2
Zenisek, D.3
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41
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12844265252
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A dynamic actin cytoskeleton functions at multiple stages of clathrin-mediated endocytosis
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Yarar D., Waterman-Storer C.M., and Schmid S.L. A dynamic actin cytoskeleton functions at multiple stages of clathrin-mediated endocytosis. Mol Biol Cell 16 (2005) 964-975
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(2005)
Mol Biol Cell
, vol.16
, pp. 964-975
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Yarar, D.1
Waterman-Storer, C.M.2
Schmid, S.L.3
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42
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4644280545
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The stimulatory action of amphiphysin on dynamin function is dependent on lipid bilayer curvature
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Yoshida Y., Kinuta M., Abe T., Liang S., Araki K., Cremona O., Di Paolo G., Moriyama Y., Yasuda T., De Camilli P., et al. The stimulatory action of amphiphysin on dynamin function is dependent on lipid bilayer curvature. Embo J 23 (2004) 3483-3491
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(2004)
Embo J
, vol.23
, pp. 3483-3491
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Yoshida, Y.1
Kinuta, M.2
Abe, T.3
Liang, S.4
Araki, K.5
Cremona, O.6
Di Paolo, G.7
Moriyama, Y.8
Yasuda, T.9
De Camilli, P.10
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43
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33745747117
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Roux A, Uyhazi K, Frost A, De Camilli P: GTP-dependent twisting of dynamin implicates constriction and tension in membrane fission. Nature, in press. See Update.
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