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4 Publications

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    03/03/15 | Profile of Eric Betzig, Stefan Hell, and W. E. Moerner, 2014 Nobel Laureates in Chemistry.
    Lippincott-Schwartz J
    Proceedings of the National Academy of Sciences of the United States of America. 2015 Mar 3;112(9):2630-2. doi: 10.1073/pnas.1500784112
    02/16/15 | Early steps in primary cilium assembly require EHD1/EHD3-dependent ciliary vesicle formation.
    Lu Q, Insinna C, Ott C, Stauffer J, Pintado PA, Rahajeng J, Baxa U, Walia V, Cuenca A, Hwang Y, Daar IO, Lopes S, Lippincott-Schwartz J, Jackson PK, Caplan S, Westlake CJ
    Nature Cell Biology. 2015 Feb 16;17(4):228-40. doi: 10.1038/ncb3109

    Membrane association with mother centriole (M-centriole) distal appendages is critical for ciliogenesis initiation. How the Rab GTPase Rab11–​Rab8 cascade functions in early ciliary membrane assembly is unknown. Here, we show that the membrane shaping proteins ​EHD1 and ​EHD3, in association with the Rab11–​Rab8 cascade, function in early ciliogenesis. ​EHD1 and ​EHD3 localize to preciliary membranes and the ciliary pocket. EHD-dependent membrane tubulation is essential for ciliary vesicle formation from smaller distal appendage vesicles (DAVs). Importantly, this step functions in M-centriole to basal body transformation and recruitment of transition zone proteins and ​IFT20. ​SNAP29, a SNARE membrane fusion regulator and ​EHD1-binding protein, is also required for DAV-mediated ciliary vesicle assembly. Interestingly, only after ciliary vesicle assembly is ​Rab8 activated for ciliary growth. Our studies uncover molecular mechanisms informing a previously uncharacterized ciliogenesis step, whereby ​EHD1 and ​EHD3 reorganize the M-centriole and associated DAVs before coordinated ciliary membrane and axoneme growth.

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    02/05/15 | Deacetylation of nuclear LC3 drives autophagy initiation under starvation.
    Huang R, Xu Y, Wan W, Shou X, Qian J, You Z, Liu B, Chang C, Zhou T, Lippincott-Schwartz J, Liu W
    Molecular cell. 2015 Feb 5;57(3):456-66. doi: 10.1016/j.molcel.2014.12.013

    Shuttling of macromolecules between different cellular compartments helps regulate the timing and extent of different cellular activities. Here, we report that LC3, a key initiator of autophagy that cycles between the nucleus and cytoplasm, becomes selectively activated in the nucleus during starvation through deacetylation by the nuclear deacetylase Sirt1. Deacetylation of LC3 at K49 and K51 by Sirt1 allows LC3 to interact with the nuclear protein DOR and return to the cytoplasm with DOR, where it is able to bind Atg7 and other autophagy factors and undergo phosphatidylethanolamine conjugation to preautophagic membranes. The association of deacetylated LC3 with autophagic factors shifts LC3's distribution from the nucleus toward the cytoplasm. Thus, an acetylation-deacetylation cycle ensures that LC3 effectively redistributes in an activated form from nucleus to cytoplasm, where it plays a central role in autophagy to enable the cell to cope with the lack of external nutrients.

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    01/01/15 | Photocontrollable fluorescent proteins for superresolution imaging.
    Shcherbakova DM, Sengupta P, Lippincott-Schwartz J, Verkhusha VV
    Annual review of biophysics. 2014;43:303-29. doi: 10.1146/annurev-biophys-051013-022836

    Superresolution fluorescence microscopy permits the study of biological processes at scales small enough to visualize fine subcellular structures that are unresolvable by traditional diffraction-limited light microscopy. Many superresolution techniques, including those applicable to live cell imaging, utilize genetically encoded photocontrollable fluorescent proteins. The fluorescence of these proteins can be controlled by light of specific wavelengths. In this review, we discuss the biochemical and photophysical properties of photocontrollable fluorescent proteins that are relevant to their use in superresolution microscopy. We then describe the recently developed photoactivatable, photoswitchable, and reversibly photoswitchable fluorescent proteins, and we detail their particular usefulness in single-molecule localization-based and nonlinear ensemble-based superresolution techniques. Finally, we discuss recent applications of photocontrollable proteins in superresolution imaging, as well as how these applications help to clarify properties of intracellular structures and processes that are relevant to cell and developmental biology, neuroscience, cancer biology and biomedicine.

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