Zobrazeno 1 - 10
of 111
pro vyhledávání: '"Samara L. Reck-Peterson"'
Autor:
Martin J. Egan, Mark A. McClintock, Ian H.L. Hollyer, Hunter L. Elliott, Samara L. Reck-Peterson
Publikováno v:
Cell Reports, Vol 11, Iss 2, Pp 201-209 (2015)
Eukaryotes have evolved multiple strategies for maintaining cellular protein homeostasis. One such mechanism involves neutralization of deleterious protein aggregates via their defined spatial segregation. Here, using the molecular disaggregase Hsp10
Externí odkaz:
https://doaj.org/article/45e68f48247f467183caaf3c6c0f161b
Publikováno v:
eLife, Vol 12 (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. Previously we reported
Externí odkaz:
https://doaj.org/article/4bd943e978794483b3f735335788a310
Autor:
Donté Alexander Stevens, Christopher Beierschmitt, Swetha Mahesula, Miles R Corley, John Salogiannis, Brian V Tsu, Bryant Cao, Andrew P Ryan, Hiroyuki Hakozawki, Samara L Reck-Peterson, Matthew D Daugherty
Publikováno v:
eLife, Vol 11 (2022)
Viruses interact with the intracellular transport machinery to promote viral replication. Such host–virus interactions can drive host gene adaptation, leaving signatures of pathogen-driven evolution in host genomes. Here, we leverage these genetic
Externí odkaz:
https://doaj.org/article/e59611f3ae034a729149b9fc1746e00b
Autor:
John P Gillies, Janice M Reimer, Eva P Karasmanis, Indrajit Lahiri, Zaw Min Htet, Andres E Leschziner, Samara L Reck-Peterson
Publikováno v:
eLife, Vol 11 (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 mot
Externí odkaz:
https://doaj.org/article/0c338fe5a65746bb99102d46fccf8b0d
Autor:
Jenna R Christensen, Agnieszka A Kendrick, Joey B Truong, Adriana Aguilar-Maldonado, Vinit Adani, Monika Dzieciatkowska, Samara L Reck-Peterson
Publikováno v:
eLife, Vol 10 (2021)
In eukaryotic cells, intracellular components are organized by the microtubule motors cytoplasmic dynein-1 (dynein) and kinesins, which are linked to cargos via adaptor proteins. While ~40 kinesins transport cargo toward the plus end of microtubules,
Externí odkaz:
https://doaj.org/article/294a1afff82f4aa8a80f8ea2d97296b4
Publikováno v:
Annual Review of Cell and Developmental Biology. 38:155-178
Eukaryotic cells across the tree of life organize their subcellular components via intracellular transport mechanisms. In canonical transport, myosin, kinesin, and dynein motor proteins interact with cargos via adaptor proteins and move along filamen
Publikováno v:
Molecular Biology of the Cell. 34
In the filamentous fungus Aspergillus nidulans, peroxisomes move by hitchhiking on early endosomes. Here, it is shown that the Woronin body, a peroxisome-derived organelle that plugs incomplete septa upon injury to hyphae, also hitchhikes on early en
The proper functioning of organelles depends on their intracellular localization, mediated by motor protein-dependent transport on cytoskeletal tracks. Rather than directly associating with a motor protein, peroxisomes move by hitchhiking on motile e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4bcd01cd81e03e0d2faa0baf24be4247
https://doi.org/10.1101/2023.01.20.524968
https://doi.org/10.1101/2023.01.20.524968
Publikováno v:
Biophysical Journal. 120:4918-4931
Cellular functions such as autophagy, cell signaling and vesicular trafficking involve the retrograde transport of motor-driven cargo along microtubules. Typically, newly formed cargo engages in slow diffusive movement from its point of origin before