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  1. AU="Tran, Phuoc Tien"
  2. AU="Alban Jonchère"
  3. AU="Ravi Varma Aithabathula"
  4. AU="Suter, Martin"
  5. AU="Chugunov, Konstantin V"
  6. AU="Moshkdanian, Ghazale"
  7. AU="Phuangthong, Chelsea"
  8. AU="Schiro, B J"
  9. AU="Chu, Dan"
  10. AU="Muhanna, Adel"
  11. AU="Ankit Mittal"
  12. AU="Dos Santos Costa Maldonado, Izabel Regina"
  13. AU="Mohamed El-Hadidi"
  14. AU="Crespo, Raquel"
  15. AU="Cozzolino, Marica"
  16. AU="Bao, Hongwei"
  17. AU="Golling, T."
  18. AU="Young, Jonathan R"
  19. AU="Lee, Jae Young"
  20. AU="Deng, Xing-Wang"
  21. AU="Wiarda, Grant"
  22. AU="Pereira, Naveen"
  23. AU="Garriga, Anna"
  24. AU="PLK. Priyadarsini"
  25. AU="Nicole E. Edgar"
  26. AU=Fredrick Kurt
  27. AU="Rowe, Mike"
  28. AU="Imannezhad, Shima"
  29. AU="DiTullio, Giacomo R"
  30. AU="Padrick, Shae B"
  31. AU="Vachiraarunwong, Arpamas"
  32. AU="Mohammad-Najar, Narges"
  33. AU="Sarica, Kemal"
  34. AU="Lescure, Alain"
  35. AU="Darawan Rinchai"
  36. AU="Sarah K McKenzie"
  37. AU="Joseph Edgar Blais"
  38. AU="Garate, Jose Antonio"

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  1. Artikel ; Online: Lis1 Has Two Opposing Modes of Regulating Cytoplasmic Dynein.

    DeSantis, Morgan E / Cianfrocco, Michael A / Htet, Zaw Min / Tran, Phuoc Tien / Reck-Peterson, Samara L / Leschziner, Andres E

    Cell

    2017  Band 170, Heft 6, Seite(n) 1197–1208.e12

    Abstract: Regulation is central to the functional versatility of cytoplasmic dynein, a motor involved in intracellular transport, cell division, and neurodevelopment. Previous work established that Lis1, a conserved regulator of dynein, binds to its motor domain ... ...

    Abstract Regulation is central to the functional versatility of cytoplasmic dynein, a motor involved in intracellular transport, cell division, and neurodevelopment. Previous work established that Lis1, a conserved regulator of dynein, binds to its motor domain and induces a tight microtubule-binding state in dynein. The work we present here-a combination of biochemistry, single-molecule assays, and cryoelectron microscopy-led to the surprising discovery that Lis1 has two opposing modes of regulating dynein, being capable of inducing both low and high affinity for the microtubule. We show that these opposing modes depend on the stoichiometry of Lis1 binding to dynein and that this stoichiometry is regulated by the nucleotide state of dynein's AAA3 domain. The low-affinity state requires Lis1 to also bind to dynein at a novel conserved site, mutation of which disrupts Lis1's function in vivo. We propose a new model for the regulation of dynein by Lis1.
    Mesh-Begriff(e) 1-Alkyl-2-acetylglycerophosphocholine Esterase/chemistry ; 1-Alkyl-2-acetylglycerophosphocholine Esterase/metabolism ; Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Cryoelectron Microscopy ; Dyneins/chemistry ; Dyneins/metabolism ; Humans ; Microtubule-Associated Proteins/chemistry ; Microtubule-Associated Proteins/metabolism ; Models, Molecular ; Molecular Motor Proteins/metabolism ; Protein Domains ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/metabolism ; Sequence Alignment
    Chemische Substanzen KIP2 protein, S cerevisiae ; Microtubule-Associated Proteins ; Molecular Motor Proteins ; Saccharomyces cerevisiae Proteins ; Adenosine Triphosphate (8L70Q75FXE) ; 1-Alkyl-2-acetylglycerophosphocholine Esterase (EC 3.1.1.47) ; PAFAH1B1 protein, S cerevisiae (EC 3.1.1.47) ; PAFAH1B1 protein, human (EC 3.1.1.47) ; Dyneins (EC 3.6.4.2)
    Sprache Englisch
    Erscheinungsdatum 2017-09-05
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ZDB-ID 187009-9
    ISSN 1097-4172 ; 0092-8674
    ISSN (online) 1097-4172
    ISSN 0092-8674
    DOI 10.1016/j.cell.2017.08.037
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: Hook3 is a scaffold for the opposite-polarity microtubule-based motors cytoplasmic dynein-1 and KIF1C.

    Kendrick, Agnieszka A / Dickey, Andrea M / Redwine, William B / Tran, Phuoc Tien / Vaites, Laura Pontano / Dzieciatkowska, Monika / Harper, J Wade / Reck-Peterson, Samara L

    The Journal of cell biology

    2019  Band 218, Heft 9, Seite(n) 2982–3001

    Abstract: The unidirectional and opposite-polarity microtubule-based motors, dynein and kinesin, drive long-distance intracellular cargo transport. Cellular observations suggest that opposite-polarity motors may be coupled. We recently identified an interaction ... ...

    Abstract The unidirectional and opposite-polarity microtubule-based motors, dynein and kinesin, drive long-distance intracellular cargo transport. Cellular observations suggest that opposite-polarity motors may be coupled. We recently identified an interaction between the cytoplasmic dynein-1 activating adaptor Hook3 and the kinesin-3 KIF1C. Here, using in vitro reconstitutions with purified components, we show that KIF1C and dynein/dynactin can exist in a complex scaffolded by Hook3. Full-length Hook3 binds to and activates dynein/dynactin motility. Hook3 also binds to a short region in the "tail" of KIF1C, but unlike dynein/dynactin, this interaction does not activate KIF1C. Hook3 scaffolding allows dynein to transport KIF1C toward the microtubule minus end, and KIF1C to transport dynein toward the microtubule plus end. In cells, KIF1C can recruit Hook3 to the cell periphery, although the cellular role of the complex containing both motors remains unknown. We propose that Hook3's ability to scaffold dynein/dynactin and KIF1C may regulate bidirectional motility, promote motor recycling, or sequester the pool of available dynein/dynactin activating adaptors.
    Mesh-Begriff(e) Cell Line, Tumor ; Dyneins/genetics ; Dyneins/metabolism ; Humans ; Kinesins/genetics ; Kinesins/metabolism ; Microtubule-Associated Proteins/genetics ; Microtubule-Associated Proteins/metabolism ; Microtubules/genetics ; Microtubules/metabolism
    Chemische Substanzen KIF1C protein, human ; Microtubule-Associated Proteins ; hook3 protein, human ; Dyneins (EC 3.6.4.2) ; Kinesins (EC 3.6.4.4)
    Sprache Englisch
    Erscheinungsdatum 2019-07-18
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.201812170
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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    ab Jg. 2022: Lesesaal (EG)

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  3. Artikel ; Online: The human cytoplasmic dynein interactome reveals novel activators of motility.

    Redwine, William B / DeSantis, Morgan E / Hollyer, Ian / Htet, Zaw Min / Tran, Phuoc Tien / Swanson, Selene K / Florens, Laurence / Washburn, Michael P / Reck-Peterson, Samara L

    eLife

    2017  Band 6

    Abstract: In human cells, cytoplasmic dynein-1 is essential for long-distance transport of many cargos, including organelles, RNAs, proteins, and viruses, towards microtubule minus ends. To understand how a single motor achieves cargo specificity, we identified ... ...

    Abstract In human cells, cytoplasmic dynein-1 is essential for long-distance transport of many cargos, including organelles, RNAs, proteins, and viruses, towards microtubule minus ends. To understand how a single motor achieves cargo specificity, we identified the human dynein interactome by attaching a promiscuous biotin ligase ('BioID') to seven components of the dynein machinery, including a subunit of the essential cofactor dynactin. This method reported spatial information about the large cytosolic dynein/dynactin complex in living cells. To achieve maximal motile activity and to bind its cargos, human dynein/dynactin requires 'activators', of which only five have been described. We developed methods to identify new activators in our BioID data, and discovered that ninein and ninein-like are a new family of dynein activators. Analysis of the protein interactomes for six activators, including ninein and ninein-like, suggests that each dynein activator has multiple cargos.
    Sprache Englisch
    Erscheinungsdatum 2017-07-18
    Erscheinungsland England
    Dokumenttyp Journal Article
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.28257
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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