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{"title"=>"Dynamin-Catalyzed Membrane Fission Requires Coordinated GTP Hydrolysis", "type"=>"journal", "authors"=>[{"first_name"=>"Ya Wen", "last_name"=>"Liu", "scopus_author_id"=>"26660602900"}, {"first_name"=>"Juha Pekka", "last_name"=>"Mattila", "scopus_author_id"=>"55989191000"}, {"first_name"=>"Sandra L.", "last_name"=>"Schmid", "scopus_author_id"=>"7202754276"}], "year"=>2013, "source"=>"PLoS ONE", "identifiers"=>{"issn"=>"19326203", "scopus"=>"2-s2.0-84873208803", "pui"=>"368246904", "doi"=>"10.1371/journal.pone.0055691", "isbn"=>"1932-6203", "sgr"=>"84873208803", "pmid"=>"23383266"}, "id"=>"078bd349-898c-3a94-a1ab-c5e58182232f", "abstract"=>"Dynamin is the most-studied membrane fission machinery and has served as a paradigm for studies of other fission GTPases; however, several critical questions regarding its function remain unresolved. In particular, because most dynamin GTPase domain mutants studied to date equally impair both basal and assembly-stimulated GTPase activities, it has been difficult to distinguish their respective roles in clathrin-mediated endocytosis (CME) or in dynamin catalyzed membrane fission. Here we compared a new dynamin mutant, Q40E, which is selectively impaired in assembly-stimulated GTPase activity with S45N, a GTP-binding mutant equally defective in both basal and assembly-stimulated GTPase activities. Both mutants potently inhibit CME and effectively recruit other endocytic accessory proteins to stalled coated pits. However, the Q40E mutant blocks at a later step than S45N, providing additional evidence that GTP binding and/or basal GTPase activities of dynamin are required throughout clathrin coated pit maturation. Importantly, using in vitro assays for assembly-stimulated GTPase activity and membrane fission, we find that the latter is much more potently inhibited by both dominant-negative mutants than the former. These studies establish that efficient fission from supported bilayers with excess membrane reservoir (SUPER) templates requires coordinated GTP hydrolysis across two rungs of an assembled dynamin collar.", "link"=>"http://www.mendeley.com/research/dynamincatalyzed-membrane-fission-requires-coordinated-gtp-hydrolysis", "reader_count"=>29, "reader_count_by_academic_status"=>{"Researcher"=>6, "Student > Ph. D. Student"=>16, "Student > Postgraduate"=>3, "Student > Master"=>3, "Student > Bachelor"=>1}, "reader_count_by_user_role"=>{"Researcher"=>6, "Student > Ph. D. Student"=>16, "Student > Postgraduate"=>3, "Student > Master"=>3, "Student > Bachelor"=>1}, "reader_count_by_subject_area"=>{"Biochemistry, Genetics and Molecular Biology"=>3, "Agricultural and Biological Sciences"=>23, "Neuroscience"=>1, "Chemistry"=>2}, "reader_count_by_subdiscipline"=>{"Neuroscience"=>{"Neuroscience"=>1}, "Chemistry"=>{"Chemistry"=>2}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>23}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>3}}, "reader_count_by_country"=>{"United Kingdom"=>2}, "group_count"=>3}

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• http://doi.org/10.1371/journal.pbio.2005377
• http://doi.org/10.1007/s12038-017-9680-y
• http://doi.org/10.15252/embj.201694613
• http://doi.org/10.1016/j.celrep.2014.06.054
• http://doi.org/10.1038/s41598-018-29001-9
• http://doi.org/10.1111/tra.12116
• http://doi.org/10.1074/jbc.M113.490474
• http://doi.org/10.1371/journal.pone.0185639
• http://doi.org/10.7554/eLife.25197
• http://doi.org/10.1091/mbc.e14-07-1240
• http://doi.org/10.1016/j.bpj.2019.09.042

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Figshare

• {"files"=>["https://ndownloader.figshare.com/files/481020"], "description"=>"<div><p>Dynamin is the most-studied membrane fission machinery and has served as a paradigm for studies of other fission GTPases; however, several critical questions regarding its function remain unresolved. In particular, because most dynamin GTPase domain mutants studied to date equally impair both basal and assembly-stimulated GTPase activities, it has been difficult to distinguish their respective roles in clathrin-mediated endocytosis (CME) or in dynamin catalyzed membrane fission. Here we compared a new dynamin mutant, Q40E, which is selectively impaired in assembly-stimulated GTPase activity with S45N, a GTP-binding mutant equally defective in both basal and assembly-stimulated GTPase activities. Both mutants potently inhibit CME and effectively recruit other endocytic accessory proteins to stalled coated pits. However, the Q40E mutant blocks at a later step than S45N, providing additional evidence that GTP binding and/or basal GTPase activities of dynamin are required throughout clathrin coated pit maturation. Importantly, using <em>in vitro</em> assays for assembly-stimulated GTPase activity and membrane fission, we find that the latter is much more potently inhibited by both dominant-negative mutants than the former. These studies establish that efficient fission from supported bilayers with excess membrane reservoir (SUPER) templates requires coordinated GTP hydrolysis across two rungs of an assembled dynamin collar.</p> </div>", "links"=>[], "tags"=>["dynamin-catalyzed", "membrane", "fission", "requires", "coordinated", "gtp", "hydrolysis"], "article_id"=>155256, "categories"=>["Biochemistry", "Cell Biology", "Biophysics"], "users"=>["Ya-Wen Liu", "Juha-Pekka Mattila", "Sandra L. Schmid"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0055691"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Dynamin_Catalyzed_Membrane_Fission_Requires_Coordinated_GTP_Hydrolysis__/155256", "title"=>"Dynamin-Catalyzed Membrane Fission Requires Coordinated GTP Hydrolysis", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-01-31 01:27:36"}
• {"files"=>["https://ndownloader.figshare.com/files/497607"], "description"=>"<p>(A) Steady-state basal GTP hydrolysis of 0.5 µM WT or mutant dynamin-1 was measured at 37°C with different concentrations of GTP. Results shown are the specific GTPase activity for each condition, and data are average ± std. dev. from 3 independent experiments. (B) Membrane fission activity of the indicated concentrations of WT or mutant dynamin-1 was determined by its ability to release vesicles from SUPER templates. Fission activity is expressed as a fraction of the total membrane released from the SUPER templates during a 30 min incubation at room temperature, as described in <i>Experimental Procedures</i>. (C) The tubulation of SUPER templates by 1 µM WT or mutant dynamin-1 after incubation for 10 min at room temperature in the absence of GTP was determined by fluorescence microscopy. Images are inverted in contrast for clarity. Scale bar, 10 µm. (D) Dominant-negative effect on clathrin-mediated endocytosis. tTA-HeLa cells acutely expressing the indicated dynamins were incubated with BSSTfn for 3 min at 37°C. The efficiency of BSSTfn internalization was determined by its inaccessibility to quenching reagent, either avidin or MesNa, and normalized to dynamin-1 WT expressing cells. Data are average ± std. dev. from 3 independent experiments.</p>", "links"=>[], "tags"=>["properties", "q40e", "s45n", "dynamin"], "article_id"=>168122, "categories"=>["Biochemistry", "Cell Biology", "Biophysics"], "users"=>["Ya-Wen Liu", "Juha-Pekka Mattila", "Sandra L. Schmid"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0055691.g001"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Biochemical_properties_of_Q40E_and_S45N_dynamin_mutants_/168122", "title"=>"Biochemical properties of Q40E and S45N dynamin mutants.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-01-31 02:15:22"}
• {"files"=>["https://ndownloader.figshare.com/files/497719"], "description"=>"<p>Indirect immunofluorescence of mouse fibroblasts acutely expressing the indicated HA-tagged dynamins, detected with anti-HA antibody (rabbit Y11, Santa Cruz or mouse 12CA5). (A) AP2 was detected with anti-α-adaptin Ab AP.6. (B), Snx9 was detected with anti-Snx9 Ab (Schmid lab) (C) Arp2/3 was detected with anti-Arp3 Ab (BD Transduction Lab). Scale bar, 10 µm. Representative cells from three independent experiments are shown.</p>", "links"=>[], "tags"=>["endocytic", "intermediates", "cells", "expressing", "dominant-negative", "dynamin"], "article_id"=>168234, "categories"=>["Biochemistry", "Cell Biology", "Biophysics"], "users"=>["Ya-Wen Liu", "Juha-Pekka Mattila", "Sandra L. Schmid"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0055691.g002"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Accumulation_of_endocytic_intermediates_in_cells_expressing_dominant_negative_dynamin_mutants_/168234", "title"=>"Accumulation of endocytic intermediates in cells expressing dominant-negative dynamin mutants.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-01-31 02:17:14"}
• {"files"=>["https://ndownloader.figshare.com/files/497828"], "description"=>"<p>(A) Thin sections of tTA-HeLa cells acutely overexpressing the indicated dynamin-1 were prepared and imaged as described in <i>Experimental Procedures</i>. Scale bar, 250 nm. Representative cells from two independent experiments are shown. (B) Quantitation of CCP intermediates. Clathrin coated endocytic intermediates were counted and scored as shallow, invaginated, elongated or internalized structures. The results are expressed as % of total CCPs scored (n). (C) The average diameter of elongated necks (n = 30) detected in cells expressing S45N (28.0±4.7 nm) or Q40E (21.7±4.8 nm) was measured. The difference is significant, <i>p</i><0.01 by Student <i>t-test</i>.</p>", "links"=>[], "tags"=>["clathrin", "coated", "pits", "accumulated", "dynamin", "mutant"], "article_id"=>168345, "categories"=>["Biochemistry", "Cell Biology", "Biophysics"], "users"=>["Ya-Wen Liu", "Juha-Pekka Mattila", "Sandra L. Schmid"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0055691.g003"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Ultrastructural_analysis_of_clathrin_coated_pits_CCPs_accumulated_in_dynamin_mutant_cells_/168345", "title"=>"Ultrastructural analysis of clathrin coated pits (CCPs) accumulated in dynamin mutant cells.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-01-31 02:19:05"}
• {"files"=>["https://ndownloader.figshare.com/files/497910"], "description"=>"<p>The inhibitory effects of increasing concentrations of S45N (A) and Q40E (B) mutants on the assembly-stimulated GTPase (•) and fission, i.e. the release of vesicles from SUPER templates (□) activities of 0.5 µM WT dynamin-1. The data (averages ± std. dev., n = 3 for GTPase assays, n = 11 for fission assays) are normalized to the activity of WT dynamin-1 alone and plotted as a function of the mutant∶WT ratio. Both assays were performed at room temperature in the presence of 1 mM GTP. (C) The inhibitory effects of the Q40E (▪) and S45N (□) mutants on the fission activity of WT dynamin-1, plotted as a function of the fraction of mutant dimers, assuming a binomial distribution. (D) Illustration of a dynamin collar formed by a 1∶1 mixture of mutant∶WT dynamin dimers. Under these conditions fission activity is inhibited ∼80% by S45N mutant and ∼60% by the Q40E mutant.</p>", "links"=>[], "tags"=>["inhibitory", "dominant-negative", "dynamin"], "article_id"=>168430, "categories"=>["Biochemistry", "Cell Biology", "Biophysics"], "users"=>["Ya-Wen Liu", "Juha-Pekka Mattila", "Sandra L. Schmid"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0055691.g004"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_In_vitro_inhibitory_effects_of_dominant_negative_dynamin_mutants_/168430", "title"=>"<i>In vitro</i> inhibitory effects of dominant-negative dynamin mutants.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-01-31 02:20:30"}
• {"files"=>["https://ndownloader.figshare.com/files/497978"], "description"=>"<p>Michaelis-Menten constants for WT and mutant dynamin-1.</p>", "links"=>[], "tags"=>["constants", "wt", "mutant"], "article_id"=>168497, "categories"=>["Biochemistry", "Cell Biology", "Biophysics"], "users"=>["Ya-Wen Liu", "Juha-Pekka Mattila", "Sandra L. Schmid"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0055691.t001"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Michaelis_Menten_constants_for_WT_and_mutant_dynamin_1_/168497", "title"=>"Michaelis-Menten constants for WT and mutant dynamin-1.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-01-31 02:21:37"}

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• {"unique-ip"=>"4", "full-text"=>"4", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"1", "cited-by"=>"0", "year"=>"2018", "month"=>"11"}
• {"unique-ip"=>"6", "full-text"=>"7", "pdf"=>"3", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"2"}
• {"unique-ip"=>"1", "full-text"=>"1", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"3"}
• {"unique-ip"=>"5", "full-text"=>"5", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"4"}
• {"unique-ip"=>"5", "full-text"=>"5", "pdf"=>"2", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"5"}
• {"unique-ip"=>"5", "full-text"=>"4", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"8"}
• {"unique-ip"=>"5", "full-text"=>"4", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"9"}
• {"unique-ip"=>"7", "full-text"=>"7", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"10"}

Relative Metric

{"start_date"=>"2013-01-01T00:00:00Z", "end_date"=>"2013-12-31T00:00:00Z", "subject_areas"=>[{"subject_area"=>"/Biology and life sciences", "average_usage"=>[269, 466, 588, 697, 800, 896, 988, 1076, 1165, 1254, 1340, 1417]}, {"subject_area"=>"/Biology and life sciences/Biochemistry", "average_usage"=>[266, 468, 593, 703, 804, 903, 993, 1084, 1171, 1256, 1339, 1422, 1492]}, {"subject_area"=>"/Engineering and technology", "average_usage"=>[254, 440, 558, 675, 785, 883, 972, 1061, 1154, 1248, 1336, 1414, 1489]}, {"subject_area"=>"/Engineering and technology/Membrane technology", "average_usage"=>[247, 423, 532, 631, 744, 843, 936, 1021, 1119, 1218, 1316, 1385, 1440, 1495]}, {"subject_area"=>"/Engineering and technology/Structural engineering", "average_usage"=>[255, 409, 496, 603, 740, 827, 921, 990, 1113, 1222, 1350, 1419, 1476, 1587]}, {"subject_area"=>"/Physical sciences", "average_usage"=>[254, 431, 547, 651, 748, 842, 932, 1017, 1098, 1178, 1259, 1336, 1404]}]}

F1000Prime