Reck-Peterson lab members shown in bold.
2023
Kusakci E, Htet ZM, Zhao Y, Gillies JP, Reck-Peterson SL, Yildiz A. (2023) Lis1 slows force-induced detachment of cytoplasmic dynein from microtubules. Nat Chem Biol. doi: 10.1038/s41589-023-01464-6. [pdf]
Also on bioRxiv: doi.org/10.1101/2022.06.02.494578
Karasmanis EP*, Reimer JM*, Kendrick AA*, Nguyen Kendrick HV, Rodriguez JA, Truong JB, Lahiri I, Reck-Peterson SL‡, and Leschziner AE‡. (2023) Lis1 relieves cytoplasmic dynein-1 auto-inhibition by acting as a molecular wedge. Nat Struct Mol Biol. 30: 1357-1364. [pdf]
Also on bioRxiv: doi.org/10.1101/2022.10.10.511666
Commentary: Lau, CK. (2023) New pieces for the Lis-dynein puzzle. Nat Struct Mol Biol. 30: 1244-1246. [pdf]
Rangan KJ‡ and Reck-Peterson, SL‡. (2023) RNA recoding in cephalopods tailors microtubule motor protein function. Cell 186: 2531-2543. [pdf]
Also on bioRxiv: doi.org/10.1101/2022.09.25.509396
Commentary : Koenig, KM. (2023) Chilling with cephalopods: Temperature-responsive RNA editing in octopus and squid. Cell 186: 2518-2520. [pdf]
KPBS video: [you tube link]
Songster LD, Bhuyan D, Christensen JR‡, Reck-Peterson SL‡. (2023) Woronin bodies move dynamically and bidirectionally by hitchhiking on early endosomes in Aspergillus nidulans. Mol. Biol. Cell 34(7):br9. doi: 10.1091/mbc.E23-01-0025. [pdf]
Also on bioRxiv: doi.org/10.1101/2023.01.20.524968
Reimer JM, DeSantis ME, Reck-Peterson SL‡, and Leschziner AE‡. (2023) Structures of human cytoplasmic dynein in complex with the lissencephaly 1 protein, LIS1. eLife, doi: 10.7554/eLife.84302. [pdf]
Also on bioRxiv: doi.org/10.1101/2022.10.08.511426
Reimer JM, Dickey AM**, Lin YX**, Abrisch RG**, Mathea S, Chatterjee D, Fay EJ, Knapp S, Daugherty MD, Reck-Peterson SL‡, and Leschziner AE‡. (2023) Structure of LRRK1 and mechanisms of autoinhibition and activation. [pdf]
Also on bioRxiv: doi.org/10.1101/2022.11.22.517582
2022
Snead DM*, Matyszewski M*, Dickey AM*, Lin YX, Leschziner AL‡, Reck-Peterson SL‡. (2022) Structural basis for Parkinson’s Disease-linked LRRK2’s binding to microtubules. Nat Struct Mol Biol. 12: 1196-1207. [pdf]
Also on bioRxiv: doi.org/10.1101/2022.01.21.477284
Stevens DA*, Beierschmitt C*, Mahesula S, Corley MR, Salogiannis J, Tsu BV, Cao B, Ryan AP, Hakozawki H, Reck-Peterson SL‡, and Daugherty MD‡. (2022) Antiviral function and viral antagonism of the rapidly evolving dynein activating adaptor NINL. eLife: 10.7554/eLife.81606. [pdf]
Also on bioRxiv: doi.org/10.1101/2022.07.11.499552
Christensen JR‡ and Reck-Peterson SL‡. (2022) Hitchhiking across kingdoms: co-transport of cargos in fungal, animal, and plant cells. Ann Rev Cell Dev Biol., doi: 10.1146/annurev-cellbio-120420-104341. [pdf]
Gillies JP*, Reimer JM*, Karasmanis EP*, Lahiri I, Htet ZM, Leschziner AE‡, Reck-Peterson SL‡. (2022) Structural basis for cytoplasmic dynein-1 regulation by Lis1. Elife. 10.7554. [link]
Also on bioRxiv: doi.org/10.1101/2021.06.11.448119
2021
Christensen JR*, Kendrick AA*, Truong JB, Aguilar-Maldonado A, Adani V, Dzieciatkowska M, Reck-Peterson SL. (2021) Cytoplasmic dynein-1 cargo diversity is mediated by the combinatorial assembly of FTS-Hook-FHIP complexes. Elife. 10:e74538. [link]
Also on bioRxiv: doi.org/10.1101/2021.10.07.463551
Triclin S, Inoue D, Gaillard J, Htet ZM, DeSantis ME, Portran D, Derivery E, Aumeier C, Schaedel L, John K, Leterrier C, Reck-Peterson SL, Blanchoin L, Théry M. (2021) Self-repair protects microtubules from destruction by molecular motors. Nat Mater. 20(6):883-891. [link]
Also on bioRxiv: doi.org/10.1101/499020
Leschziner AE*, Reck-Peterson SL*. (2021) Structural Biology of LRRK2 and its Interaction with Microtubules. Mov Disord. 36(11):2494-2504. [link]
Mogre SS, Christensen JR, Reck-Peterson SL, Koslover EF. (2021) Optimizing microtubule arrangements for rapid cargo capture. Biophys J. 16;120(22):4918-4931. [link]
Also on bioRxiv: doi.org/10.1101/2021.06.02.446824
Salogiannis J*, Christensen JR*, Songster LD, Aguilar-Maldonado A, Shukla N, Reck-Peterson SL. (2021) Regulation of peroxisome and lipid droplet hitchhiking by PxdA and the DipA phosphatase. MBoC: [pdf]
2020
Deniston CK*, Salogiannis J*, Mathea S*, Snead DM, Lahiri I, Matyszewski M, Donosa O, Watanabe R, Bohning J, Shiau AK, Knapp S, Villa E, Reck-Peterson SL‡, Leschziner AL‡. (2020) Structure of LRRK2 in Parkinson’s disease and model for microtubule interaction. Nature: 588:344-349. [pdf]
Htet ZM*, Gillies JP*, Baker RW, Leschziner AL, DeSantis ME‡, Reck-Peterson SL‡. (2020) Lis1 promotes the formation of maximally activated cytoplasmic dynein-1 complexes. Nat Cell Biol. 5: 518-525. [pdf]
Commentary on this research appeared in: Nat Cell Biol. 22: 515-517. [pdf]
Mogre SS, Christensen JR, Reck-Peterson SL, Koslovar EF. (2020) Hitching a Ride: Mechanics of Organelle Transport Through Linker-Mediated Hitchhiking. Biophysical Journal 118: 1357-1369. [pdf]
Also on bioRxiv: doi.org/10.1101/811372
2019
Cao Y, Ghabache E, Miao Y, Niman C, Hakozaki H, Reck-Peterson SL, Devreotes PN, Rappel WJ. (2019) A minimal computational model for three-dimensional cell migration. J R Soc Interface 16(161): 20190619. [pdf]
Kendrick AA, Dickey AM**, Redwine WB**, Tran PT, Pontano Vaites L, Dzieciatkowska M, Harper JW, and Reck-Peterson SL. (2019) HOOK3 is a scaffold for the opposite-polarity microtubule-based motors cytoplasmic dynein-1 and KIF1C. J Cell Biol. 218: 2982-3001. [pdf]
Also on bioRxiv: doi.org/10.1101/508887
2018
Reck-Peterson SL‡, Redwine WB, Vale RD. Carter AP‡. (2018) The cytoplasmic dynein transport machinery and its many cargoes. Nat Rev Mol Cell Biol 19: 382-398. DOI: 10.1038/s41580-018-0004-3. [pdf]
2017
DeSantis ME*, Cianfrocco MA*, Htet ZA*, Tran PT, Reck-Peterson SL‡, Leschziner AE‡. (2017) Lis1 has two opposing modes of regulating cytoplasmic dynein. Cell 170: 1197-1208. [pdf]
Also on bioRxiv: doi.org/10.1101/152645
Redwine WB*, DeSantis, ME*, Hollyer I, Htet ZM, Tran PT, Swanson SK, Florens L, Washburn MP, Reck-Peterson SL. (2017) The human cytoplasmic dynein interactome reveals novel activators of motility. eLife: 6:e28257. [pdf]
Also on bioRxiv: doi.org/10.1101/143743
Lippert LG, Dadosh T, Hadden JA, Karnawat V, Diroll BT, Murray CB, Holzbaur ELF, Schulten K, Reck-Peterson SL, Goldman YE. (2017) Angular measurements of the dynein ring reveal a stepping mechanism dependent on a flexible stalk. PNAS: 114: E4564-E4573. [pdf]
Salogiannis J and Reck-Peterson SL. (2017) Hitchhiking: A Non-Canonical Mode of Microtubule-Based Transport.Trends Cell Biol 27: 141-150. [pdf]
2016
Salogiannis J, Egan MJ, Reck-Peterson SL. (2016) Peroxisomes move by hitchhiking on early endosomes using the novel linker proteins PxdA. J Cell Biol 212: 289-296. [pdf]
Also on bioRxiv: doi.org/10.1101/034231
Commentary on this research appeared in:
In this issue: Short B. (2016) PxdA helps peroxisomes hitch a ride. J Cell Biol 212: 258. [pdf]
Research highlight: Strzyz P. (2016) How peroxisomes hitchhike on endosomes. Nat Rev Mol Cell Biol 17: 134.
2015
Cianfrocco MA*, DeSantis ME*, Leschziner AE, Reck-Peterson SL. (2015) Mechanism and Regulation of Cytoplasmic Dynein. Annu Rev Cell Dev Biol 31: 83-108. [pdf]
Egan MJ*, McClintock MA*, Hollyer IH, Elliott HL, Reck-Peterson SL. (2015) Cytoplasmic dynein is required for the spatial organization of protein aggregates in filamentous fungi. Cell Reports 11: 201-209. [pdf]
Reck-Peterson SL. (2015) Dynactin Revealed. Nat Struct Mol Biol. 22: 359-360. [pdf]
2014
Downes DJ, Chonofsky M, Tan K, Pfannenstiel BT, Reck-Peterson SL, Todd RB. (2014) Characterization of the Mutagenic Spectrum of 4-Nitroquinoline 1-Oxide (4-NQO) in Aspergillus nidulans by Whole Genome Sequencing. G3 4: 2483-2492. [pdf]
Toropova K*, Zou S*, Roberts AJ, Redwine WB, Goodman BS, Reck-Peterson SL‡, Leschziner AE‡. (2014) Lis1 regulates dynein by sterically blocking its mechanochemical cycle. eLIFE 3:e03372. [pdf]
Cheng L, Desai J, Miranda CJ, Duncan JS, Qiu W, Nugent AA, Kolpak AL, Wu CC, Drokhlyansky E, Delisle MM, Chan W, Wei Y, Propst F, Reck-Peterson SL, Fritzsch B, Engle EC. (2014) Human CFEOM1 mutations attenuate KIF21A autoinhibition and cause oculomotor axon stalling. Neuron 82: 334-349. [pdf]
Reck-Peterson SL. (2014) Molecular motors: shifting gears with light. Nat Nanotech 9: 661-662. [pdf]
Roberts AJ, Goodman BS, Reck-Peterson SL. (2014) Reconstitution of dynein transport to the microtubule plus end by kinesin. eLIFE 3:e02641. [pdf]
Tan K, Roberts AJ, Chonofsky M, Egan MJ, Reck-Peterson SL. (2014) A microscopy-based screen employing multiplex genome sequencing identifies cargo-specific requirements for dynein velocity. Mol Biol Cell 25: 669-678. [pdf]
Goodman BS and Reck-Peterson SL. (2014) Engineering defined motor ensembles with DNA origami. Methods in Enzymology 540: 169-188. [pdf]
2013
Reck-Peterson SL. (2013) Teaming up: from motors to people. Mol. Biol. Cell. 24: 3267-3269. [pdf]
2012
Egan MJ, McClintock MA, Reck-Peterson SL. (2012) Microtubule-based transport in filamentous fungi. Curr Opin Microbiol 15: 637-645. [pdf]
Derr ND*, Goodman BS*, Jungmann R, Leschziner AE, Shih WM, Reck-Peterson SL. (2012) Tug of war in motor protein ensembles revealed with a programmable DNA origmai scaffold. Science 338: 662-665. [pdf]
Commentary on this research appeared in: Science 338: 626-627. [pdf]
Goodman BS, Derr ND, Reck-Peterson SL. (2012) Engineered, harnessed, and hijacked: synthetic uses for cytoskeletal systems. Trends Cell Biol 22: 644-652. [pdf]
Redwine WB*, Hernandez-Lopez R*, Zou S, Huang J, Reck-Peterson SL, Leschziner AE. (2012) Structural basis for microtubule binding and release by dynein.Science 337: 1532-1536. [pdf]
Huang J*, Roberts AJ*, Leschziner AE, Reck-Peterson SL. (2012) Lis1 acts as a "clutch" between the ATPase and microtubule-binding domains of the dynein motor. Cell 150: 975-986. [pdf]
Commentary on this research appeared in Cell 150: 877-879 [pdf]
Egan M, Tan K, Reck-Peterson SL. (2012) Lis1 is an initiation factor for dynein-driven organelle transport. J Cell Biol 197: 971-982. [pdf]
Commentary on this research appeared in: J Cell Biol 197: 852. [pdf]
Laan L, Pavin N, Husson J, Romet-Lemonne G, van Duin M, Lopez MP, Vale RD, Julicher F, Reck-Peterson SL, Dogterom M. (2012) “Cortical” dynein controls microtubule dynamics and length, generating pulling forces that reliably position microtubule asters. Cell 148: 502-514. [pdf]
Qiu W*, Derr ND*, Goodman BS, Villa E, Wu D, Shih W, Reck-Peterson SL. (2012) Dynein achieves processive motion using both stochastic and coordinated stepping. Nat Struct Mol Biol 19: 193-200. [pdf]
Commentary on this research appeared in: Nature 482: 7383. [pdf]
2011 and earlier
Reck-Peterson SL, Vale RD, Gennerich A. (2011) Motile properties of cytoplasmic dynein. In “Handbook of dynein.” Pan Stanford Publishing. Editors: Keiko Hirose and Linda Amos. [pdf]
Zhang J, Tan K, Wu X, Chen G, Sun J, Reck-Peterson SL, Hammer J, Xiang X. (2011) Aspergillus myosin-V supports polarized growth in the absence of microtubule-based transport. PLoS One 6: e28575. [pdf]
Su X, Qiu W, Gupta ML, Pereira-Leal JB, Reck-Peterson SL, Pellman D. (2011) Mechanism underlying the dual-mode regulation of microtubule dynamics by Kip3/kinesin-8. Mol Cell 43: 751-763. [pdf]
Gennerich A, and Reck-Peterson SL. (2011) Probing the force generation and stepping behavior of cytoplasmic dynein. Methods Mol Biol 783: 63-80. [pdf]
Reck-Peterson SL, Derr N, Stuurman N. (2010) Single molecule imaging using total internal reflection microscopy. In “Live Cell Imaging: a laboratory manual”, 2nd edition. Cold Spring Harbor Press. [pdf]
Postdoctoral work
Kardon J, Reck-Peterson SL, Vale RD. (2009) Regulation of the processivity and intracellular localization of S. cerevisiae dynein by dynactin. PNAS 106: 5669-74. [pdf]
Cho C, Reck-Peterson SL, Vale RD. (2008) Cytoplasmic dynein's regulatory ATPase sites affect processivity and force generation. J Biol Chem 283: 25839-45. [pdf]
Gennerich A, Carter AP, Reck-Peterson SL, Vale RD. (2007) Force-induced bidirectional stepping of cytoplasmic dynein. Cell 131: 952-965. [pdf]
Reck-Peterson SL, Yildiz Y**, Carter AP**, Gennerich A, Zhang N, and Vale RD. (2006) Single molecule analysis of dynein processivity and stepping behavior.Cell 126: 335-348. [pdf]
Commentaries on this research appeared in: Cell 126: 242-244 [pdf], Nat Rev Mol Cell Biol 7: 625 [pdf], J Cell Biol 172: 486-492 [pdf]
*co-first author; **co-second author; ‡co-corresponding author
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