Structural Insights into Triglyceride Storage Mediated by Fat Storage-Inducing Transmembrane (FIT) Protein 2
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{"title"=>"Structural insights into triglyceride storage mediated by fat storage-inducing transmembrane (FIT) protein 2", "type"=>"journal", "authors"=>[{"first_name"=>"David A.", "last_name"=>"Gross", "scopus_author_id"=>"7401437819"}, {"first_name"=>"Erik L.", "last_name"=>"Snapp", "scopus_author_id"=>"6603016324"}, {"first_name"=>"David L.", "last_name"=>"Silver", "scopus_author_id"=>"7202150869"}], "year"=>2010, "source"=>"PLoS ONE", "identifiers"=>{"scopus"=>"2-s2.0-77956509037", "pui"=>"359515631", "doi"=>"10.1371/journal.pone.0010796", "issn"=>"19326203", "isbn"=>"1932-6203", "pmid"=>"20520733", "sgr"=>"77956509037"}, "id"=>"da0a2f0a-6b50-3778-b6b1-0f628e9af13b", "abstract"=>"Fat storage-Inducing Transmembrane proteins 1 & 2 (FIT1/FITM1 and FIT2/FITM2) belong to a unique family of evolutionarily conserved proteins localized to the endoplasmic reticulum that are involved in triglyceride lipid droplet formation. FIT proteins have been shown to mediate the partitioning of cellular triglyceride into lipid droplets, but not triglyceride biosynthesis. FIT proteins do not share primary sequence homology with known proteins and no structural information is available to inform on the mechanism by which FIT proteins function. Here, we present the experimentally-solved topological models for FIT1 and FIT2 using N-glycosylation site mapping and indirect immunofluorescence techniques. These methods indicate that both proteins have six-transmembrane-domains with both N- and C-termini localized to the cytosol. Utilizing this model for structure-function analysis, we identified and characterized a gain-of-function mutant of FIT2 (FLL(157-9)AAA) in transmembrane domain 4 that markedly augmented the total number and mean size of lipid droplets. Using limited-trypsin proteolysis we determined that the FLL(157-9)AAA mutant has enhanced trypsin cleavage at K86 relative to wild-type FIT2, indicating a conformational change. Taken together, these studies indicate that FIT2 is a 6 transmembrane domain-containing protein whose conformation likely regulates its activity in mediating lipid droplet formation.", "link"=>"http://www.mendeley.com/research/structural-insights-triglyceride-storage-mediated-fat-storageinducing-transmembrane-fit-protein-2", "reader_count"=>30, "reader_count_by_academic_status"=>{"Student > Doctoral Student"=>4, "Researcher"=>11, "Student > Ph. D. Student"=>7, "Other"=>2, "Student > Master"=>1, "Student > Bachelor"=>2, "Lecturer"=>1, "Professor"=>1}, "reader_count_by_user_role"=>{"Student > Doctoral Student"=>4, "Researcher"=>11, "Student > Ph. D. Student"=>7, "Other"=>2, "Student > Master"=>1, "Student > Bachelor"=>2, "Lecturer"=>1, "Professor"=>1}, "reader_count_by_subject_area"=>{"Biochemistry, Genetics and Molecular Biology"=>6, "Agricultural and Biological Sciences"=>18, "Medicine and Dentistry"=>4, "Chemistry"=>1}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>4}, "Chemistry"=>{"Chemistry"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>18}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>6}}, "reader_count_by_country"=>{"United States"=>1, "Finland"=>1}, "group_count"=>1}

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/847590"], "description"=>"<p><b>A</b>, Indirect immunofluorescence microscopy of FIT2-V5 FNF insertions. Cells expressing various FIT2-V5 FNF mutants were fixed, permeabilized with digitonin with or without Triton X-100, and were incubated with FLAG antibody to detect the FLAG epitope. Cytosolic-oriented loops are detected in digitonin-permeabilized cells. Luminal-oriented loops are detected in cells permeablized with Triton X-100. <b>B</b>, Indirect immunofluorescence microscopy of FIT1-V5 FNF insertions. Cells were treated as in <b>A</b>, except that cells expressing FIT1-V5 without an FNF insertion were incubated with a V5 antibody to determine the orientation of the C-terminus. Images are representative of three independent experiments (scale bar: 5 µm).</p>", "links"=>[], "tags"=>["Biochemistry", "cell biology", "biochemistry/cell signaling and trafficking structures", "biochemistry/membrane proteins and energy transduction", "diabetes and endocrinology/obesity"], "article_id"=>518046, "categories"=>["Biochemistry", "Computational Biology", "Cell Biology"], "users"=>["David A. Gross", "Erik L. Snapp", "David L. Silver"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0010796.g002", "stats"=>{"downloads"=>0, "page_views"=>2, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Figure_2_/518046", "title"=>"Figure 2", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2010-05-24 02:14:06"}
  • {"files"=>["https://ndownloader.figshare.com/files/847869"], "description"=>"<p>FLL(157-9)AAA FIT2 (FLL) and FIT2 (WT) were transfected into cells and limited trypsin digestion time-courses were performed on both of these constructs. Results were analyzed by Western blot using antibodies directed to the luminal loop 2 of FIT2 (designated anti-LL2) and the C-terminus (designated anti-C-term). FLL was expressed to similar levels as WT (lanes 1 and 2). Two proteolytic products were detected and designated P1 and P2. The amount of P2 is increased for FLL following trypsin digestion. As a control for the efficiency of digestion of each construct, blots were reprobed with the anti-C-term antibody (lower panel) that detects the cytosolic-localized FIT2 C-terminus. FL designates full length FIT2. The Western blots shown are representative of three independent experiments.</p>", "links"=>[], "tags"=>["fit2", "altered", "conformation", "compared", "wild-type"], "article_id"=>518316, "categories"=>["Biochemistry", "Computational Biology", "Cell Biology"], "users"=>["David A. Gross", "Erik L. Snapp", "David L. Silver"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0010796.g005", "stats"=>{"downloads"=>0, "page_views"=>8, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_FLL_157_9_AAA_FIT2_has_an_altered_conformation_compared_to_wild_type_FIT2_/518316", "title"=>"FLL(157-9)AAA FIT2 has an altered conformation compared to wild-type FIT2.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2010-05-24 02:18:36"}
  • {"files"=>["https://ndownloader.figshare.com/files/847756"], "description"=>"<p><b>A</b>, Confocal fluorescence microscopy of lipid droplets in HEK293 cells transiently transfected with wild-type FIT2-V5 (WT), FLL(157-9)AAA FIT2-V5 (designated FLL), human DGAT2, or mock transfected control. Images are representative of three independent experiments. Cells were stained for lipid droplets (green) and FIT2-V5 (red), and nuclei (blue). <b>B</b>, Histogram of lipid droplet volumes. HEK293 cells were set up as in <b>A</b> and subjected to confocal fluorescence microscopy. Z-stacks were captured and 3D renderings were constructed. Data was analyzed using Velocity software (Perkin Elmer). Analysis was performed on 10 independent 3D renderings from three independent experiments. <b>C</b>, Quantification of lipid droplets per cell is shown (mock vs WT*, FLL**, and DGAT2***: p<3×10<sup>−4</sup>, 2.5×10<sup>−5</sup>, 4.9×10<sup>−7</sup>, respectively). The data are presented as mean ± s.d. <b>D</b>, Quantification of cellular triglyceride concentration in cells expressing the indicated constructs. DGAT2 or mock transfected were used as positive and negative controls, respectively. The data are presented as fold-increase over mock control and are representative of three independent transfections.</p>", "links"=>[], "tags"=>["fit2-v5", "gain-of-function"], "article_id"=>518216, "categories"=>["Biochemistry", "Computational Biology", "Cell Biology"], "users"=>["David A. Gross", "Erik L. Snapp", "David L. Silver"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0010796.g004", "stats"=>{"downloads"=>2, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_FLL_157_9_AAA_FIT2_V5_is_a_gain_of_function_mutant_/518216", "title"=>"FLL(157-9)AAA FIT2-V5 is a gain-of-function mutant.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2010-05-24 02:16:56"}
  • {"files"=>["https://ndownloader.figshare.com/files/847678"], "description"=>"<p>Alignment of partial sequences of FIT2 and FIT1 from various species showing the “FIT signature sequence” is indicated within the red box. The most conserved group of residues in this domain comprises the FLL sequence, whose hydrophobic character was retained throughout evolution. Based on our experimentally determined topological model of FIT proteins (<a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0010796#pone-0010796-g001\" target=\"_blank\">Figure 1</a> and <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0010796#pone-0010796-g002\" target=\"_blank\">2</a>), the FIT signature sequence is located in transmembrane domain 4.</p>", "links"=>[], "tags"=>["conserved", "tract", "amino", "acids", "transmembrane"], "article_id"=>518133, "categories"=>["Biochemistry", "Computational Biology", "Cell Biology"], "users"=>["David A. Gross", "Erik L. Snapp", "David L. Silver"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0010796.g003", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_A_conserved_tract_of_amino_acids_in_transmembrane_domain_4_of_FITs_/518133", "title"=>"A conserved tract of amino acids in transmembrane domain 4 of FITs.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2010-05-24 02:15:33"}
  • {"files"=>["https://ndownloader.figshare.com/files/847450"], "description"=>"<p><b>A and C</b>, FIT2 and FIT1 topological models with N- and C-termini oriented toward the cytosol and six transmembrane domains with a large second luminal loop. The amino acid positions of insertion of FNF tags for the determination of topology by glycosylation site mapping and indirect immunofluorescence are indicated. As indicated, all constructs contain C-terminal V5 and polyhistidine epitope tags. <b>B and D</b>, Increased molecular weights of specific FNF-V5 constructs relative to wild-type FIT2 or FIT1 (indicated by asterisks) detected by Western blot analysis indicated potential glycosylation and luminal orientation. Decreased molecular weight of constructs following PGNaseF treatment indicated glycosylation and luminal orientation. Asterisks indicate glycosylated forms of FIT2 and FIT1 constructs. The multiple asterisks indicated for the FIT2 construct 51 is due to two tandem FNF glycosylation sites inserted into that construct (arrow indicates non-glycosylated construct 51). B and D are representative of two independent experiments.</p>", "links"=>[], "tags"=>["topology", "murine", "fit2"], "article_id"=>517903, "categories"=>["Biochemistry", "Computational Biology", "Cell Biology"], "users"=>["David A. Gross", "Erik L. Snapp", "David L. Silver"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0010796.g001", "stats"=>{"downloads"=>0, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Membrane_topology_of_murine_FIT2_and_FIT1_/517903", "title"=>"Membrane topology of murine FIT2 and FIT1.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2010-05-24 02:11:43"}
  • {"files"=>["https://ndownloader.figshare.com/files/422091", "https://ndownloader.figshare.com/files/422125", "https://ndownloader.figshare.com/files/422176", "https://ndownloader.figshare.com/files/422227", "https://ndownloader.figshare.com/files/422265"], "description"=>"<div><p>Fat storage-Inducing Transmembrane proteins 1 & 2 (FIT1/FITM1 and FIT2/FITM2) belong to a unique family of evolutionarily conserved proteins localized to the endoplasmic reticulum that are involved in triglyceride lipid droplet formation. FIT proteins have been shown to mediate the partitioning of cellular triglyceride into lipid droplets, but not triglyceride biosynthesis. FIT proteins do not share primary sequence homology with known proteins and no structural information is available to inform on the mechanism by which FIT proteins function. Here, we present the experimentally-solved topological models for FIT1 and FIT2 using N-glycosylation site mapping and indirect immunofluorescence techniques. These methods indicate that both proteins have six-transmembrane-domains with both N- and C-termini localized to the cytosol. Utilizing this model for structure-function analysis, we identified and characterized a gain-of-function mutant of FIT2 (FLL(157-9)AAA) in transmembrane domain 4 that markedly augmented the total number and mean size of lipid droplets. Using limited-trypsin proteolysis we determined that the FLL(157-9)AAA mutant has enhanced trypsin cleavage at K86 relative to wild-type FIT2, indicating a conformational change. Taken together, these studies indicate that FIT2 is a 6 transmembrane domain-containing protein whose conformation likely regulates its activity in mediating lipid droplet formation.</p></div>", "links"=>[], "tags"=>["insights", "triglyceride", "mediated", "storage-inducing", "transmembrane"], "article_id"=>143357, "categories"=>["Biochemistry", "Biological Sciences", "Cell Biology"], "users"=>["David A. Gross", "Erik L. Snapp", "David L. Silver"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0010796.s001", "https://dx.doi.org/10.1371/journal.pone.0010796.s002", "https://dx.doi.org/10.1371/journal.pone.0010796.s003", "https://dx.doi.org/10.1371/journal.pone.0010796.s004", "https://dx.doi.org/10.1371/journal.pone.0010796.s005"], "stats"=>{"downloads"=>0, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Structural_Insights_into_Triglyceride_Storage_Mediated_by_Fat_Storage_Inducing_Transmembrane_FIT_Protein_2/143357", "title"=>"Structural Insights into Triglyceride Storage Mediated by Fat Storage-Inducing Transmembrane (FIT) Protein 2", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2010-05-24 00:55:57"}
  • {"files"=>["https://ndownloader.figshare.com/files/847939"], "description"=>"<p><b>A</b>, Cells were set up as in <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0010796#pone-0010796-g005\" target=\"_blank\">Fig. 5</a> by expressing either K240A, K256A, R257A (all constructs are V5 tagged) and compared to wild-type FIT2-V5 (WT) in limited trypsin digestion time course assays as indicated. Additional bands were detected with the anti-LL2 antibody due to the presence of lysine and arginine residues in the C-terminal V5 tag. Note the molecular weight shift in the P1 fragment of K256A and R257A, but not of K240A, indicating that K256 or R257 are likely cleavage sites giving rise to P1. Also of note is the lower amount of P2 generated in these mutants compared to wild-type correlating with lower expression levels of these constructs. <b>B</b>, Cells were set up as in <b>A</b> to examine the tryptic pattern of K86A, R92A and R93A compared to wild-type. Of note are the decreased molecular weights of the P2 fragments of K86A and R92A, but not of R93A compared to WT, indicating that cleavage likely occurs at K86 (and K256/R257) to generate the P2 fragment. <b>C</b>, Cells were set up as in <b>A and B</b>. K177A or K180A did not affect the size of P2, indicating that these residues are not cleaved by trypsin in WT FIT2. <b>D</b>, Topological model showing the possible cytosolic trypsin-susceptible residues of FIT2 in the limited trypsin digestion assay. Based on the above data, residues in red indicate those that are cleaved to form proteolytic products P1 and P2. Residues in blue are those that are not cleaved by trypsin in wild-type FIT2. These data are representative of two independent experiments.</p>", "links"=>[], "tags"=>["p1", "p2", "trypsin", "cleavage"], "article_id"=>518396, "categories"=>["Biochemistry", "Computational Biology", "Cell Biology"], "users"=>["David A. Gross", "Erik L. Snapp", "David L. Silver"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0010796.g006", "stats"=>{"downloads"=>1, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Mutational_analysis_to_define_the_P1_and_P2_fragment_trypsin_cleavage_sites_/518396", "title"=>"Mutational analysis to define the P1 and P2 fragment trypsin cleavage sites.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2010-05-24 02:19:56"}
  • {"files"=>["https://ndownloader.figshare.com/files/848027"], "description"=>"<p>The FIT2 FLL mutant has an altered conformation relative to wild-type FIT2 that results in increased solvent accessibility of residues in cytosolic loop 2 containing residue K86. This conformational change may facilitate increased partitioning of triglyceride into nascent cytosolic lipid droplets or allow for the creation of larger lipid droplets by undetermined mechanisms.</p>", "links"=>[], "tags"=>["conformational", "fit2", "fll"], "article_id"=>518486, "categories"=>["Biochemistry", "Computational Biology", "Cell Biology"], "users"=>["David A. Gross", "Erik L. Snapp", "David L. Silver"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0010796.g007", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Model_for_conformational_change_in_FIT2_FLL_mutant_/518486", "title"=>"Model for conformational change in FIT2 FLL mutant.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2010-05-24 02:21:26"}

PMC Usage Stats | Further Information

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Relative Metric

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