Results 11 to 20 of about 8,015 (203)

Structural basis for cytoplasmic dynein-1 regulation by Lis1 [PDF]

eLife, 2022
The lissencephaly 1 gene, LIS1, is mutated in patients with the neurodevelopmental disease lissencephaly. The Lis1 protein is conserved from fungi to mammals and is a key regulator of cytoplasmic dynein-1, the major minus-end-directed microtubule motor ...
John P Gillies, Janice M Reimer, Eva P Karasmanis, Indrajit Lahiri, Zaw Min Htet, Andres E Leschziner, Samara L Reck-Peterson   +6 more
doaj   +3 more sources

Molecular mechanism of dynein-dynactin complex assembly by LIS1 [PDF]

Science
Cytoplasmic dynein is a microtubule motor vital for cellular organization and division. It functions as a ~4-megadalton complex containing its cofactor dynactin and a cargo-specific coiled-coil adaptor. However, how dynein and dynactin recognize diverse adaptors, how they interact with each other during complex formation, and the role of critical ...
Kashish Singh, Clinton K Lau, Giulia Manigrasso   +2 more
exaly   +4 more sources

HIV-1 Tat interacts with LIS1 protein [PDF]

Retrovirology, 2005
Background HIV-1 Tat activates transcription of HIV-1 viral genes by inducing phosphorylation of the C-terminal domain (CTD) of RNA polymerase II (RNAPII).
Turner Willie, Lane William S, Voloshin Yaroslav, Sapir Tamar, Ammosova Tatyana, Epie Nicolas, Reiner Orly, Nekhai Sergei   +7 more
doaj   +3 more sources

Altered extracellular matrix structure and elevated stiffness in a brain organoid model for disease [PDF]

Nature Communications
The viscoelastic properties of tissues influence their morphology and cellular behavior, yet little is known about changes in these properties during brain malformations.
Maayan Karlinski Zur, Bidisha Bhattacharya, Inna Solomonov, Sivan Ben Dror, Alon Savidor, Yishai Levin, Amir Prior, Tamar Sapir, Talia Harris, Tsviya Olender, Rita Schmidt, J. M. Schwarz, Irit Sagi, Amnon Buxboim, Orly Reiner   +14 more
doaj   +2 more sources

LncRNA RASAL2-AS1 promotes METTL14-mediated m6A methylation in the proliferation and progression of head and neck squamous cell carcinoma [PDF]

Cancer Cell International
Background Long non-coding RNAs (lncRNAs) are key regulators of the 6-methyladenosine (m6A) epigenetic modification, playing a role in the initiation and progression of tumors.
Meiting Rong, Ming Zhang, Feihong Dong, Ke Wu, Bingkun Cai, Jinrui Niu, Le Yang, Zhongyan Li, Hui-yi Lu   +8 more
doaj   +2 more sources

Cancer Stem Cells Shift Metabolite Acetyl-Coenzyme A to Abrogate the Differentiation of CD103⁺ T Cells. [PDF]

Adv Sci (Weinh)
Lei et al. demonstrate that cancer stem cells (CSCs) play a pivotal role in impairing the differentiation of CD103+ T cells in patients with non‐small‐cell lung cancer. The key mechanism involves CSC‐derived acetyl‐CoA, which disrupts CD103+ T cell differentiation by sequentially inducing acetylation and ubiquitination of the Blimp‐1 protein. Targeting
Lei J, Ji H, Guo J, Liu M, Su D, Zheng Y, Xu L, Cao Q, Ren T, Gui J, Wen Z.   +10 more
europepmc   +2 more sources

LIS1 and NDEL1 Regulate Axonal Trafficking of Mitochondria in Mature Neurons

Frontiers in Molecular Neuroscience, 2022
Defective mitochondrial dynamics in axons have been linked to both developmental and late-onset neurological disorders. Axonal trafficking is in large part governed by the microtubule motors kinesin-1 and cytoplasmic dynein 1 (dynein).
Jai P. Pandey, Liang Shi, Remi A. Brebion, Deanna S. Smith   +3 more
doaj   +1 more source

Structures of human dynein in complex with the lissencephaly 1 protein, LIS1

eLife, 2023
The lissencephaly 1 protein, LIS1, is mutated in type-1 lissencephaly and is a key regulator of cytoplasmic dynein-1. At a molecular level, current models propose that LIS1 activates dynein by relieving its autoinhibited form.
Janice M Reimer, Morgan E DeSantis, Samara L Reck-Peterson, Andres E Leschziner   +3 more
doaj   +1 more source

Two microtubule-plus-end binding proteins LIS1-1 and LIS1-2, homologues of human LIS1 in Neurospora crassa [PDF]

Fungal Genetics and Biology, 2015
LIS1 is a microtubule (Mt) plus-end binding protein that interacts with the dynein/dynactin complex. In humans, LIS1 is required for proper nuclear and organelle migration during cell growth. Although gene duplication is absent from Neurospora crassa, we found two paralogues of human LIS1.
Callejas-Negrete, Olga A, Plamann, Michael, Schnittker, Robert, Bartnicki-García, Salomon, Roberson, Robert W, Pimienta, Genaro, Mouriño-Pérez, Rosa R   +6 more
openaire   +4 more sources

CENP-F stabilizes kinetochore-microtubule attachments and limits dynein stripping of corona cargoes [PDF]

, 2020
Accurate chromosome segregation demands efficient capture of microtubules by kinetochores and their conversion to stable bioriented attachments that can congress and then segregate chromosomes.
Allan, Andrew D. McAinsh, Auckland, Bancroft, Baumbach, Berto, Berto, Bolhy, Bomont, Chan, Ciossani, Currie, DeSantis, Dix, Dudka, Emanuele Roscioli, Etemad, Faulkner, Feng, Filges, Gama, Gassmann, Gutierrez, Haley, Helena Louise Elvidge Coker, Helgeson, Hoffman, Holt, Howell, Huang, Huis In ’t Veld, Johnson, Kanfer, Kanfer, Klinman, Kuhn, Liu, Magidson, Magidson, Maiato, McEwen, McEwen, McKinley, Meraldi, Monda, Moughamian, Musacchio, Musacchio, Musinipally, Olenick, Olziersky, Pandey, Pereira, Peterka, Philip Auckland, Raaijmakers, Ran, Rattner, Rodriguez-Rodriguez, Roscioli, Sacristan, Samejima, Schmidt, Shao, Shrestha, Siller, Simões, Stehman, Tai, Thrower, Toropova, Vagnoni, Vergnolle, Volkov, Wojcik, Wynne, Wynne, Wynne, Yang, Yi, Zhu   +80 more
core   +1 more source