Z
Zhanna Lipatova
Researcher at University of Illinois at Chicago
Publications - 24
Citations - 1029
Zhanna Lipatova is an academic researcher from University of Illinois at Chicago. The author has contributed to research in topics: Rab & GTPase. The author has an hindex of 17, co-authored 24 publications receiving 890 citations. Previous affiliations of Zhanna Lipatova include Stanford University.
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Journal ArticleDOI
TRAPPII subunits are required for the specificity switch of a Ypt-Rab GEF.
Nadya Morozova,Yongheng Liang,Andrei A. Tokarev,Shu H. Chen,Randal Cox,Jelena Andrejic,Zhanna Lipatova,Vicki A. Sciorra,Scott D. Emr,Nava Segev +9 more
TL;DR: It is suggested that the Trs120–Trs130 subcomplex joins TRAPP in the late Golgi to switch its GEF activity from Ypt1 to Ypt31/32, thereby coordinating Golgi entry and exit.
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Regulation of selective autophagy onset by a Ypt/Rab GTPase module
TL;DR: A Ypt/Rab module is defined—comprising an activator, GTPase, and effector—that orchestrates the onset of selective autophagy, a process vital for cell homeostasis and it is demonstrated here that YPT/Rabs can regulate two independent membrane-transport processes by recruiting process-specific effectors.
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Direct Interaction between a Myosin V Motor and the Rab GTPases Ypt31/32 Is Required for Polarized Secretion
TL;DR: Using the yeast-two hybrid system and coprecipitation of recombinant proteins, it is shown that Ypt31/32 in their guanosine triphosphate (GTP)-bound form interact directly with Myo2-GTD and this interaction is required for polarized secretion.
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TRAPP Complexes in Secretion and Autophagy
TL;DR: New information about TRAPP complexes is summarized, new insights about their function are highlighted, current controversies and future perspectives are discussed and a direct role for TRAPP as a vesicle tether is suggested.
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A Role for Macro-ER-Phagy in ER Quality Control.
Zhanna Lipatova,Nava Segev +1 more
TL;DR: It is shown that macro-ER-phagy is dependent on Atgs and Ypt GTPases and its cargo passes through APs and for the first time the role of Atg9, the only integral-membrane core Atg, is uncoupled from that of other core Atgs.