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  1. Article ; Online: Nanodisc-Based Proteomics Identify Caj1 as an Hsp40 with Affinity for Phosphatidic Acid Lipids.

    Zhang, Xiao X / Young, John William / Foster, Leonard J / Duong, Franck

    Journal of proteome research

    2021  Volume 20, Issue 10, Page(s) 4831–4839

    Abstract: Many soluble proteins interact with membranes to perform important biological functions, including signal transduction, regulation, transport, trafficking, and biogenesis. Despite their importance, these protein-membrane interactions are difficult to ... ...

    Abstract Many soluble proteins interact with membranes to perform important biological functions, including signal transduction, regulation, transport, trafficking, and biogenesis. Despite their importance, these protein-membrane interactions are difficult to characterize due to their often-transient nature as well as phospholipids' poor solubility in aqueous solution. Here, we employ nanodiscs-small, water-soluble patches of a lipid bilayer encircled with amphipathic scaffold proteins-along with quantitative proteomics to identify lipid-binding proteins in
    MeSH term(s) Calmodulin-Binding Proteins ; HSP40 Heat-Shock Proteins ; Lipid Bilayers ; Membrane Proteins ; Nanostructures ; Phosphatidic Acids ; Proteomics ; Saccharomyces cerevisiae Proteins
    Chemical Substances CAJ1 protein, S cerevisiae ; Calmodulin-Binding Proteins ; HSP40 Heat-Shock Proteins ; Lipid Bilayers ; Membrane Proteins ; Phosphatidic Acids ; Saccharomyces cerevisiae Proteins
    Language English
    Publishing date 2021-09-14
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2078618-9
    ISSN 1535-3907 ; 1535-3893
    ISSN (online) 1535-3907
    ISSN 1535-3893
    DOI 10.1021/acs.jproteome.1c00503
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Nanodisc-Based Proteomics Identify Caj1 as an Hsp40 with Affinity for Phosphatidic Acid Lipids

    Zhang, Xiao X. / Young, John William / Foster, Leonard J. / Duong, Franck

    Journal of proteome research. 2021 Sept. 14, v. 20, no. 10

    2021  

    Abstract: Many soluble proteins interact with membranes to perform important biological functions, including signal transduction, regulation, transport, trafficking, and biogenesis. Despite their importance, these protein–membrane interactions are difficult to ... ...

    Abstract Many soluble proteins interact with membranes to perform important biological functions, including signal transduction, regulation, transport, trafficking, and biogenesis. Despite their importance, these protein–membrane interactions are difficult to characterize due to their often-transient nature as well as phospholipids’ poor solubility in aqueous solution. Here, we employ nanodiscs—small, water-soluble patches of a lipid bilayer encircled with amphipathic scaffold proteins—along with quantitative proteomics to identify lipid-binding proteins in Saccharomyces cerevisiae. Using nanodiscs reconstituted with yeast total lipid extracts or only phosphatidylethanolamine (PE-nanodiscs), we capture several known membrane-interacting proteins, including the Rab GTPases Sec4 and Ypt1, which play key roles in vesicle trafficking. Utilizing PE-nanodiscs enriched with phosphatidic acid (PEPA-nanodiscs), we specifically capture a member of the Hsp40/J-protein family, Caj1, whose function has recently been linked to membrane protein quality control. We show that the Caj1 interaction with liposomes containing PA is modulated by pH and PE lipids and depends on two patches of positively charged residues near the C-terminus of the protein. The protein Caj1 is the first example of an Hsp40/J-domain protein with affinity for membranes and phosphatidic acid lipid specificity. These findings highlight the utility of combining proteomics with lipid nanodiscs to identify and characterize protein–lipid interactions that may not be evident using other methods. Data are available via ProteomeXchange with the identifier PXD027992.
    Keywords Saccharomyces cerevisiae ; aqueous solutions ; biogenesis ; guanosinetriphosphatase ; heat-shock protein 40 ; lipid bilayers ; membrane proteins ; pH ; phosphatidylethanolamines ; protein value ; proteome ; proteomics ; quality control ; research ; signal transduction ; surfactants ; water solubility ; yeasts
    Language English
    Dates of publication 2021-0914
    Size p. 4831-4839.
    Publishing place American Chemical Society
    Document type Article
    ZDB-ID 2078618-9
    ISSN 1535-3907 ; 1535-3893
    ISSN (online) 1535-3907
    ISSN 1535-3893
    DOI 10.1021/acs.jproteome.1c00503
    Database NAL-Catalogue (AGRICOLA)

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  3. Article ; Online: Nanodiscs and SILAC-based mass spectrometry to identify a membrane protein interactome.

    Zhang, Xiao X / Chan, Catherine S / Bao, Huan / Fang, Yuan / Foster, Leonard J / Duong, Franck

    Journal of proteome research

    2012  Volume 11, Issue 2, Page(s) 1454–1459

    Abstract: Integral membrane proteins are challenging to work with biochemically given their insoluble nature; the nanodisc circumvents the difficulty by stabilizing them in small patches of lipid bilayer. Here, we show that nanodiscs combined with SILAC-based ... ...

    Abstract Integral membrane proteins are challenging to work with biochemically given their insoluble nature; the nanodisc circumvents the difficulty by stabilizing them in small patches of lipid bilayer. Here, we show that nanodiscs combined with SILAC-based quantitative proteomics can be used to identify the soluble interacting partners of virtually any membrane protein. As a proof of principle, we applied the method to the bacterial SecYEG protein-conducting channel, the maltose transporter MalFGK(2) and the membrane integrase YidC. In contrast to the detergent micelles, which tend to destabilize interactions, the nanodisc was able to capture out of a complex whole cell extract the proteins SecA, Syd, and MalE with a high degree of confidence and specificity. The method was sensitive enough to isolate these interactors as a function of the lipid composition in the disc and the culture conditions. In agreement with a previous photo-cross linking analysis, YidC did not show any high-affinity interactions with cytosolic or periplasmic proteins. These three examples illustrate the utility of nanoscale lipid bilayers to identify the soluble peripheral partners of proteins intergrated in the lipid bilayer.
    MeSH term(s) Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Isotope Labeling/methods ; Lipid Metabolism ; Lipids/chemistry ; Mass Spectrometry/methods ; Membrane Proteins/chemistry ; Membrane Proteins/metabolism ; Multiprotein Complexes/chemistry ; Multiprotein Complexes/metabolism ; Nanostructures/chemistry ; Proteome/chemistry ; Proteome/metabolism ; Proteomics/methods
    Chemical Substances Bacterial Proteins ; Lipids ; Membrane Proteins ; Multiprotein Complexes ; Proteome
    Language English
    Publishing date 2012-02-03
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2078618-9
    ISSN 1535-3907 ; 1535-3893
    ISSN (online) 1535-3907
    ISSN 1535-3893
    DOI 10.1021/pr200846y
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

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  4. Article: Nanodiscs and SILAC-Based Mass Spectrometry to Identify a Membrane Protein Interactome

    Zhang, Xiao X / Bao Huan / Chan Catherine S / Duong Franck / Fang Yuan / Foster Leonard J

    Journal of Proteome Research. 2012 Feb. 03, v. 11, no. 2

    2012  

    Abstract: Integral membrane proteins are challenging to work with biochemically given their insoluble nature; the nanodisc circumvents the difficulty by stabilizing them in small patches of lipid bilayer. Here, we show that nanodiscs combined with SILAC-based ... ...

    Abstract Integral membrane proteins are challenging to work with biochemically given their insoluble nature; the nanodisc circumvents the difficulty by stabilizing them in small patches of lipid bilayer. Here, we show that nanodiscs combined with SILAC-based quantitative proteomics can be used to identify the soluble interacting partners of virtually any membrane protein. As a proof of principle, we applied the method to the bacterial SecYEG protein-conducting channel, the maltose transporter MalFGK₂ and the membrane integrase YidC. In contrast to the detergent micelles, which tend to destabilize interactions, the nanodisc was able to capture out of a complex whole cell extract the proteins SecA, Syd, and MalE with a high degree of confidence and specificity. The method was sensitive enough to isolate these interactors as a function of the lipid composition in the disc and the culture conditions. In agreement with a previous photo-cross linking analysis, YidC did not show any high-affinity interactions with cytosolic or periplasmic proteins. These three examples illustrate the utility of nanoscale lipid bilayers to identify the soluble peripheral partners of proteins intergrated in the lipid bilayer.
    Keywords detergents ; lipid bilayers ; lipid composition ; maltose ; mass spectrometry ; membrane proteins ; micelles ; proteome ; proteomics
    Language English
    Dates of publication 2012-0203
    Size p. 1454-1459.
    Publishing place American Chemical Society
    Document type Article
    ZDB-ID 2078618-9
    ISSN 1535-3907 ; 1535-3893
    ISSN (online) 1535-3907
    ISSN 1535-3893
    DOI 10.1021%2Fpr200846y
    Database NAL-Catalogue (AGRICOLA)

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  5. Article ; Online: A functional genomics screen identifying blood cell development genes in Drosophila by undergraduates participating in a course-based research experience.

    Evans, Cory J / Olson, John M / Mondal, Bama Charan / Kandimalla, Pratyush / Abbasi, Ariano / Abdusamad, Mai M / Acosta, Osvaldo / Ainsworth, Julia A / Akram, Haris M / Albert, Ralph B / Alegria-Leal, Elitzander / Alexander, Kai Y / Ayala, Angelica C / Balashova, Nataliya S / Barber, Rebecca M / Bassi, Harmanjit / Bennion, Sean P / Beyder, Miriam / Bhatt, Kush V /
    Bhoot, Chinmay / Bradshaw, Aaron W / Brannigan, Tierney G / Cao, Boyu / Cashell, Yancey Y / Chai, Timothy / Chan, Alex W / Chan, Carissa / Chang, Inho / Chang, Jonathan / Chang, Michael T / Chang, Patrick W / Chang, Stephen / Chari, Neel / Chassiakos, Alexander J / Chen, Iris E / Chen, Vivian K / Chen, Zheying / Cheng, Marsha R / Chiang, Mimi / Chiu, Vivian / Choi, Sharon / Chung, Jun Ho / Contreras, Liset / Corona, Edgar / Cruz, Courtney J / Cruz, Renae L / Dang, Jefferson M / Dasari, Suhas P / De La Fuente, Justin R O / Del Rio, Oscar M A / Dennis, Emily R / Dertsakyan, Petros S / Dey, Ipsita / Distler, Rachel S / Dong, Zhiqiao / Dorman, Leah C / Douglass, Mark A / Ehresman, Allysen B / Fu, Ivy H / Fua, Andrea / Full, Sean M / Ghaffari-Rafi, Arash / Ghani, Asmar Abdul / Giap, Bosco / Gill, Sonia / Gill, Zafar S / Gills, Nicholas J / Godavarthi, Sindhuja / Golnazarian, Talin / Goyal, Raghav / Gray, Ricardo / Grunfeld, Alexander M / Gu, Kelly M / Gutierrez, Natalia C / Ha, An N / Hamid, Iman / Hanson, Ashley / Hao, Celesti / He, Chongbin / He, Mengshi / Hedtke, Joshua P / Hernandez, Ysrael K / Hlaing, Hnin / Hobby, Faith A / Hoi, Karen / Hope, Ashley C / Hosseinian, Sahra M / Hsu, Alice / Hsueh, Jennifer / Hu, Eileen / Hu, Spencer S / Huang, Stephanie / Huang, Wilson / Huynh, Melanie / Javier, Carmen / Jeon, Na Eun / Ji, Sunjong / Johal, Jasmin / John, Amala / Johnson, Lauren / Kadakia, Saurin / Kakade, Namrata / Kamel, Sarah / Kaur, Ravinder / Khatra, Jagteshwar S / Kho, Jeffrey A / Kim, Caleb / Kim, Emily Jin-Kyung / Kim, Hee Jong / Kim, Hyun Wook / Kim, Jin Hee / Kim, Seong Ah / Kim, Woo Kyeom / Kit, Brian / La, Cindy / Lai, Jonathan / Lam, Vivian / Le, Nguyen Khoi / Lee, Chi Ju / Lee, Dana / Lee, Dong Yeon / Lee, James / Lee, Jason / Lee, Jessica / Lee, Ju-Yeon / Lee, Sharon / Lee, Terrence C / Lee, Victoria / Li, Amber J / Li, Jialing / Libro, Alexandra M / Lien, Irvin C / Lim, Mia / Lin, Jeffrey M / Liu, Connie Y / Liu, Steven C / Louie, Irene / Lu, Shijia W / Luo, William Y / Luu, Tiffany / Madrigal, Josef T / Mai, Yishan / Miya, Darron I / Mohammadi, Mina / Mohanta, Sayonika / Mokwena, Tebogo / Montoya, Tonatiuh / Mould, Dallas L / Murata, Mark R / Muthaiya, Janani / Naicker, Seethim / Neebe, Mallory R / Ngo, Amy / Ngo, Duy Q / Ngo, Jamie A / Nguyen, Anh T / Nguyen, Huy C X / Nguyen, Rina H / Nguyen, Thao T T / Nguyen, Vincent T / Nishida, Kevin / Oh, Seo-Kyung / Omi, Kristen M / Onglatco, Mary C / Almazan, Guadalupe Ortega / Paguntalan, Jahzeel / Panchal, Maharshi / Pang, Stephanie / Parikh, Harin B / Patel, Purvi D / Patel, Trisha H / Petersen, Julia E / Pham, Steven / Phan-Everson, Tien M / Pokhriyal, Megha / Popovich, Davis W / Quaal, Adam T / Querubin, Karl / Resendiz, Anabel / Riabkova, Nadezhda / Rong, Fred / Salarkia, Sarah / Sama, Nateli / Sang, Elaine / Sanville, David A / Schoen, Emily R / Shen, Zhouyang / Siangchin, Ken / Sibal, Gabrielle / Sin, Garuem / Sjarif, Jasmine / Smith, Christopher J / Soeboer, Annisa N / Sosa, Cristian / Spitters, Derek / Stender, Bryan / Su, Chloe C / Summapund, Jenny / Sun, Beatrice J / Sutanto, Christine / Tan, Jaime S / Tan, Nguon L / Tangmatitam, Parich / Trac, Cindy K / Tran, Conny / Tran, Daniel / Tran, Duy / Tran, Vina / Truong, Patrick A / Tsai, Brandon L / Tsai, Pei-Hua / Tsui, C Kimberly / Uriu, Jackson K / Venkatesh, Sanan / Vo, Maique / Vo, Nhat-Thi / Vo, Phuong / Voros, Timothy C / Wan, Yuan / Wang, Eric / Wang, Jeffrey / Wang, Michael K / Wang, Yuxuan / Wei, Siman / Wilson, Matthew N / Wong, Daniel / Wu, Elliott / Xing, Hanning / Xu, Jason P / Yaftaly, Sahar / Yan, Kimberly / Yang, Evan / Yang, Rebecca / Yao, Tony / Yeo, Patricia / Yip, Vivian / Yogi, Puja / Young, Gloria Chin / Yung, Maggie M / Zai, Alexander / Zhang, Christine / Zhang, Xiao X / Zhao, Zijun / Zhou, Raymond / Zhou, Ziqi / Abutouk, Mona / Aguirre, Brian / Ao, Chon / Baranoff, Alexis / Beniwal, Angad / Cai, Zijie / Chan, Ryan / Chien, Kenneth Chang / Chaudhary, Umar / Chin, Patrick / Chowdhury, Praptee / Dalie, Jamlah / Du, Eric Y / Estrada, Alec / Feng, Erwin / Ghaly, Monica / Graf, Rose / Hernandez, Eduardo / Herrera, Kevin / Ho, Vivien W / Honeychurch, Kaitlyn / Hou, Yurianna / Huang, Jo M / Ishii, Momoko / James, Nicholas / Jang, Gah-Eun / Jin, Daphne / Juarez, Jesse / Kesaf, Ayse Elif / Khalsa, Sat Kartar / Kim, Hannah / Kovsky, Jenna / Kuang, Chak Lon / Kumar, Shraddha / Lam, Gloria / Lee, Ceejay / Lee, Grace / Li, Li / Lin, Joshua / Liu, Josephine / Ly, Janice / Ma, Austin / Markovic, Hannah / Medina, Cristian / Mungcal, Jonelle / Naranbaatar, Bilguudei / Patel, Kayla / Petersen, Lauren / Phan, Amanda / Phung, Malcolm / Priasti, Nadiyah / Ruano, Nancy / Salim, Tanveer / Schnell, Kristen / Shah, Paras / Shen, Jinhua / Stutzman, Nathan / Sukhina, Alisa / Tian, Rayna / Vega-Loza, Andrea / Wang, Joyce / Wang, Jun / Watanabe, Rina / Wei, Brandon / Xie, Lillian / Ye, Jessica / Zhao, Jeffrey / Zimmerman, Jill / Bracken, Colton / Capili, Jason / Char, Andrew / Chen, Michel / Huang, Pingdi / Ji, Sena / Kim, Emily / Kim, Kenneth / Ko, Julie / Laput, Sean Louise G / Law, Sam / Lee, Sang Kuk / Lee, Olivia / Lim, David / Lin, Eric / Marik, Kyle / Mytych, Josh / O'Laughlin, Andie / Pak, Jensen / Park, Claire / Ryu, Ruth / Shinde, Ashwin / Sosa, Manny / Waite, Nick / Williams, Mane / Wong, Richard / Woo, Jocelyn / Woo, Jonathan / Yepuri, Vishaal / Yim, Dorothy / Huynh, Dan / Wijiewarnasurya, Dinali / Shapiro, Casey / Levis-Fitzgerald, Marc / Jaworski, Leslie / Lopatto, David / Clark, Ira E / Johnson, Tracy / Banerjee, Utpal

    G3 (Bethesda, Md.)

    2021  Volume 11, Issue 1

    Abstract: Undergraduate students participating in the UCLA Undergraduate Research Consortium for Functional Genomics (URCFG) have conducted a two-phased screen using RNA interference (RNAi) in combination with fluorescent reporter proteins to identify genes ... ...

    Abstract Undergraduate students participating in the UCLA Undergraduate Research Consortium for Functional Genomics (URCFG) have conducted a two-phased screen using RNA interference (RNAi) in combination with fluorescent reporter proteins to identify genes important for hematopoiesis in Drosophila. This screen disrupted the function of approximately 3500 genes and identified 137 candidate genes for which loss of function leads to observable changes in the hematopoietic development. Targeting RNAi to maturing, progenitor, and regulatory cell types identified key subsets that either limit or promote blood cell maturation. Bioinformatic analysis reveals gene enrichment in several previously uncharacterized areas, including RNA processing and export and vesicular trafficking. Lastly, the participation of students in this course-based undergraduate research experience (CURE) correlated with increased learning gains across several areas, as well as increased STEM retention, indicating that authentic, student-driven research in the form of a CURE represents an impactful and enriching pedagogical approach.
    MeSH term(s) Animals ; Blood Cells ; Drosophila/genetics ; Genomics/education ; Humans ; Students ; Universities
    Language English
    Publishing date 2021-02-12
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2629978-1
    ISSN 2160-1836 ; 2160-1836
    ISSN (online) 2160-1836
    ISSN 2160-1836
    DOI 10.1093/g3journal/jkaa028
    Database MEDical Literature Analysis and Retrieval System OnLINE

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