Jennifer Lippincott‐Schwartz

National Institutes of Health

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Rachid Sougrat

King Abdullah University of Science and Technology

Michal Jarník

Eunice Kennedy Shriver National Institute of Child Health and Human Development

Richard D. Klausner

Lyell Immunopharma (United States)

Lydia C. Yuan

Eunice Kennedy Shriver National Institute of Child Health and Human Development

Prabuddha Sengupta

Janelia Research Campus

Lynn Vitale‐Cross

National Institute of Dental and Craniofacial Research

James H. Hurley

University of California, Berkeley

Irwin M. Arias

National Institutes of Health

Juan S. Bonifacino

Eunice Kennedy Shriver National Institute of Child Health and Human Development

Samantha L. Deed

University of Melbourne

Cooperative Institutions

National Institutes of Health

Eunice Kennedy Shriver National Institute of Child Health and Human Development

University of Melbourne

Health and Human Development (2HD) Research Network

La Trobe University

ARC Centre of Excellence for Coherent X-ray Science

National Institute of Neurological Disorders and Stroke

National Cancer Institute

Australian Research Council

Cornell University

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LKB1/AMPK and PKA Control ABCB11 Trafficking and Polarization in Hepatocytes

PLoS ONE (2014)

László Homolya Dong Fu Prabuddha Sengupta Michal Jarník Jean‐Pierre Gillet

Polarization of hepatocytes is manifested by bile canalicular network formation and activation of LKB1 and AMPK, which control cellular energy metabolism. The bile acid, taurocholate, also regulates development of the canalicular network through activation of AMPK. In the present study, we used collagen sandwich hepatocyte cultures from control and liver-specific LKB1 knockout mice to examine the role of LKB1 in trafficking of ABCB11, the canalicular bile acid transporter. In polarized hepatocytes, ABCB11 traffics from Golgi to the apical plasma membrane and endogenously cycles through the rab 11a-myosin Vb recycling endosomal system. LKB1 knockout mice were jaundiced, lost weight and manifested impaired bile canalicular formation and intracellular trafficking of ABCB11, and died within three weeks. Using live cell imaging, fluorescence recovery after photobleaching (FRAP), particle tracking, and biochemistry, we found that LKB1 activity is required for microtubule-dependent trafficking of ABCB11 to the canalicular membrane. In control hepatocytes, ABCB11 trafficking was accelerated by taurocholate and cAMP; however, in LKB1 knockout hepatocytes, ABCB11 trafficking to the apical membrane was greatly reduced and restored only by cAMP, but not taurocholate. cAMP acted through a PKA-mediated pathway which did not activate AMPK. Our studies establish a regulatory role for LKB1 in ABCB11 trafficking to the canalicular membrane, hepatocyte polarization, and canalicular network formation.

10.1371/journal.pone.0091921

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Citations (46)

Membrane Cycling between the ER and Golgi Apparatus and Its Role in Biosynthetic Transport

Sub-cellular biochemistry/Subcellular biochemistry (1993)

Jennifer Lippincott‐Schwartz

COPI

Rab

Axoplasmic transport

Transport protein

10.1007/978-1-4615-2912-5_5

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Citations (24)

Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: Evidence for membrane cycling from Golgi to ER

Cell (1989)

Jennifer Lippincott‐Schwartz Lydia C. Yuan Juan S. Bonifacino Richard D. Klausner

Brefeldin A

Golgi membrane

Transport protein

10.1016/0092-8674(89)90685-5

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Citations (1,689)

Organization of organelles and membrane traffic by microtubules

Current Opinion in Cell Biology (1995)

Nelson B. Cole Jennifer Lippincott‐Schwartz

Organelle

10.1016/0955-0674(95)80045-x

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Citations (325)

Chapter 3 Using Photoactivatable Proteins to Monitor Autophagosome Lifetime

Methods in enzymology on CD-ROM/Methods in enzymology (2009)

Dale W. Hailey Jennifer Lippincott‐Schwartz

ATG8

Autophagosome

10.1016/s0076-6879(08)03603-3

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Citations (10)

Dynamics of Secretory Membrane Trafficking

Annals of the New York Academy of Sciences (2004)

Jennifer Lippincott‐Schwartz

The study of intracellular membrane trafficking and organelle dynamics has been revolutionized with the advent of GFP technology, which allows individual proteins to be tagged with GFP and monitored in living cells. Using GFP-based techniques such as selective photobleaching and time-lapse imaging of different GFP color variants, it is now possible to address a host of questions related to protein retention within the organelles, the origin and fate of transport intermediates, and the extent of trafficking through different transport pathways. This has provided unexpected new insights into the organization and function of secretory and endocytic pathways within cells.

Organelle

Transport protein

Photobleaching

Live cell imaging

10.1196/annals.1315.019

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Citations (18)

Electron tomography of the Maurer's cleft organelles of Plasmodium falciparum‐infected erythrocytes reveals novel structural features

Molecular Microbiology (2007)

Eric Hanssen Rachid Sougrat Sarah Frankland Samantha L. Deed Nectarios Klonis

Summary During intraerythrocytic development, the human malaria parasite, Plasmodium falciparum , establishes membrane‐bound compartments, known as Maurer's clefts, outside the confines of its own plasma membrane. The Maurer's compartments are thought to be a crucial component of the machinery for protein sorting and trafficking; however, their ultrastructure is only partly defined. We have used electron tomography to image Maurer's clefts of 3D7 strain parasites. The compartments are revealed as flattened structures with a translucent lumen and a more electron‐dense coat. They display a complex and convoluted morphology, and some regions are modified with surface nodules, each with a circular cross‐section of ∼25 nm. Individual 25 nm vesicle‐like structures are also seen in the erythrocyte cytoplasm and associated with the red blood cell membrane. The Maurer's clefts are connected to the red blood cell membrane by regions with extended stalk‐like profiles. Immunogold labelling with specific antibodies confirms differential labelling of the Maurer's clefts and the parasitophorous vacuole and erythrocyte membranes. Spot fluorescence photobleaching was used to demonstrate the absence of a lipid continuum between the Maurer's clefts and parasite membranes and the host plasma membrane.

Immunogold labelling

Organelle

Cryo-electron tomography

Compartment (ship)

10.1111/j.1365-2958.2007.06063.x

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Citations (94)

Structural basis for midbody targeting of spastin by the ESCRT‐III protein CHMP1B

The FASEB Journal (2009)

Dong Yang Neggy Rismanchi Benoît Renvoisé Jennifer Lippincott‐Schwartz Craig Blackstone

The endosomal sorting complex required for transport (ESCRT) machinery, including ESCRT‐III, localizes to the midbody and participates in the membrane‐abscission step of cytokinesis. The ESCRT‐III protein chromatin‐modifying protein 1B (CHMP1B) is required for recruitment of the MIT domain‐containing protein spastin, a microtubule‐severing enzyme, to the midbody. The 2.5‐A structure of the C‐terminal tail of CHMP1B with the MIT domain of spastin reveals a specific, high‐affinity complex involving a noncanonical binding site between the first and third helices of the MIT domain. The structural interface is twice as large as that of the MIT domain of the VPS4‐CHMP complex, consistent with the high affinity of the interaction. A series of unique hydrogen‐bonding interactions and close packing of small side chains discriminate against the other ten human ESCRT‐III subunits. Point mutants in the CHMP1B binding site of spastin block recruitment of spastin to the midbody.

Midbody

ESCRT

10.1096/fasebj.23.1_supplement.864.2

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Citations (6)

Fluorescent Proteins for Photoactivation Experiments

Methods in cell biology (2008)

Jennifer Lippincott‐Schwartz George H. Patterson

Fluorescent protein

Fluorescent labelling

10.1016/s0091-679x(08)85003-0

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Citations (90)