Molecular basis for the assembly of the dynein transport machinery on microtubules DOI Creative Commons
Qinhui Rao, Pengxin Chai, Kai Zhang

и другие.

bioRxiv (Cold Spring Harbor Laboratory), Год журнала: 2024, Номер unknown

Опубликована: Дек. 30, 2024

Abstract Cytoplasmic dynein-1, a microtubule-based motor protein, requires dynactin and an adaptor to form the processive dynein-dynactin-adaptor (DDA) complex. The role of microtubules in DDA assembly has been elusive. Here, we reveal detailed structural insights into microtubule-mediated using cryo-electron microscopy. We find that adaptor-independent dynein- complex (DD) predominantly forms on intrinsic 2:1 stoichiometry, induced by spontaneous parallelization dynein upon microtubule binding. Adaptors can squeeze exchange within assembled microtubule-bound DD complex, which is enabled relative rotations between dynactin, further facilitated light intermediate chains assist ‘search’ mechanism. Our findings elucidate dynamic adaptability transport machinery, new mode for motile

Язык: Английский

Dynein and dynactin move long-range but are delivered separately to the axon tip DOI Creative Commons
Alexander D. Fellows, Michaela Bruntraeger, Thomas Burgold

и другие.

The Journal of Cell Biology, Год журнала: 2024, Номер 223(5)

Опубликована: Фев. 6, 2024

Axonal transport is essential for neuronal survival. This driven by microtubule motors including dynein, which transports cargo from the axon tip back to cell body. function requires its cofactor dynactin and regulators LIS1 NDEL1. Due difficulties imaging dynein at a single-molecule level, it unclear how this motor coordinate along length of axon. Here, we use neuron-inducible human stem line (NGN2-OPTi-OX) endogenously tag components visualize them near-single molecule regime. In retrograde direction, find that can move entire (>500 µm). Furthermore, NDEL1 also undergo long-distance movement, despite being mainly implicated with initiation transport. Intriguingly, in anterograde dynein/LIS1 moves faster than dynactin/NDEL1, consistent on different cargos. Therefore, neurons ensure efficient holding dynein/dynactin cargos over long distances but keeping separate until required.

Язык: Английский

Процитировано

13

MINFLUX reveals dynein stepping in live neurons DOI Creative Commons
Jonas M. Schleske, Jasmine Hubrich, Jan Otto Wirth

и другие.

Proceedings of the National Academy of Sciences, Год журнала: 2024, Номер 121(38)

Опубликована: Сен. 10, 2024

Dynein is the primary molecular motor responsible for retrograde intracellular transport of a variety cargoes, performing successive nanometer-sized steps within milliseconds. Due to limited spatiotemporal precision established methods tracking, current knowledge dynein stepping essentially slowed-down measurements in vitro. Here, we use MINFLUX fluorophore localization directly track CRISPR/Cas9-tagged endogenous with nanometer/millisecond living neurons. We show that primarily takes 8 nm steps, including frequent sideways but few backward steps. Strikingly, majority direction reversals between and anterograde movement occurred on time scale single (16 ms), suggesting rapid regulatory reversal mechanism. Tug-of-war-like behavior during pauses or was unexpectedly rare. By analyzing dwell concluded rate-limiting process underlies mechanism, likely arising from just one adenosine 5′-triphosphate hydrolysis event being required each step. Our study underscores power elucidate changes underlying protein function cells.

Язык: Английский

Процитировано

6

Neural Tracing Protein‐Functionalized Nanoparticles Capable of Fast Retrograde Axonal Transport in Live Neurons DOI Creative Commons
Wenqian Wang, Md. Musfizur Hassan, Natasha Kapoor‐Kaushik

и другие.

Small, Год журнала: 2024, Номер unknown

Опубликована: Апрель 22, 2024

Neural tracing proteins like horseradish peroxidase-conjugated wheat germ agglutinin (WGA-HRP) can target the central nervous system (CNS) through anatomic retrograde transport without crossing blood-brain barrier (BBB). Conjugating WGA-HRP to nanoparticles may enable creation of BBB-bypassing nanomedicine. Microfluidics and two-photon confocal microscopy is applied screen nanocarriers for efficacy gain mechanistic insights into their interactions with neurons. Protein modification gold alters cellular uptake at axonal terminal activates fast transport. Trajectory analysis individual endosomes carrying reveals a run-and-pause pattern along axon WGA-HRP-conjugated exhibiting longer run duration faster instantaneous velocity than those nonconjugated nanoparticles. The results offer explanation different dynamics as well cell-based functional assay neuron-targeted goal developing nanomedicine treatment disorders.

Язык: Английский

Процитировано

2

MINFLUX Reveals Dynein Stepping in Live Neurons DOI Creative Commons
Jonas M. Schleske, Jasmine Hubrich, Jan Otto Wirth

и другие.

bioRxiv (Cold Spring Harbor Laboratory), Год журнала: 2024, Номер unknown

Опубликована: Май 23, 2024

Dynein is the primary molecular motor responsible for retrograde intracellular transport of a variety cargoes, performing successive nanometer-sized steps within milliseconds. Due to limited spatiotemporal precision established methods tracking, current knowledge dynein stepping essentially slowed-down measurements in vitro. Here, we use MINFLUX fluorophore localization directly track CRISPR/Cas9-tagged endogenous with nanometer/millisecond living neurons. We show that primarily takes 8 nm steps, including frequent sideways but few backward steps. Strikingly, majority direction reversals between and anterograde movement occurred on time scale single (16 ms), suggesting rapid regulatory reversal mechanism. Tug-of-war-like behavior during pauses or was unexpectedly rare. By analyzing dwell concluded rate-limiting process underlies mechanism whereby consumes one adenosine 5’-triphosphate (ATP) per step. Our study underscores power elucidate changes underlying protein function cells.

Язык: Английский

Процитировано

1

Episodic Transport of Protein Aggregates Achieves a Positive Size Selectivity in Aggresome Formation DOI Open Access
Rui Fang,

Luolan Bai,

Boyan Li

и другие.

bioRxiv (Cold Spring Harbor Laboratory), Год журнала: 2024, Номер unknown

Опубликована: Авг. 7, 2024

Eukaryotic cells direct toxic misfolded proteins to various protein quality control pathways based on their chemical features and aggregation status. Aggregated are targeted selective autophagy or specifically sequestered into the "aggresome," a perinuclear inclusion at microtubule-organizing center (MTOC). However, mechanism for selectively sequestering aggregates aggresome remains unclear. To investigate formation, we reconstituted MTOC-directed aggregate transport in

Язык: Английский

Процитировано

1

Acidic pH of Early Endosomes Governs SARS-CoV-2 Transport in Host Cells DOI Creative Commons

Perla Fares,

Mariam Duhaini,

Suvranta K. Tripathy

и другие.

Journal of Biological Chemistry, Год журнала: 2024, Номер unknown, С. 108144 - 108144

Опубликована: Дек. 1, 2024

Endocytosis is a prominent mechanism for SARS-CoV-2 entry into host cells. Upon internalization early endosomes (EEs), the virus transported to late (LEs), where acidic conditions facilitate spike protein processing and viral genome release. Dynein kinesin motors drive EE transport along microtubules; dynein moves EEs perinuclear region, while kinesins direct them towards plasma membrane, creating tug-of-war over direction of transport. Here, we identify that luminal pH key factor regulating outcome this tug-of-war. Among known endosomal regulators, only sodium-proton exchanger NHE9 has so far been genetically linked severe COVID-19 risk. functions as proton leak pathway specifically on endosomes. We show limiting acidification by increasing expression leads decreased infectivity spike-bearing in Our investigation identified membrane lipid phosphatidylinositol-3-phosphate (PI3P) link between changes Normally, mature, PI3P depletes. However, cells with high expression, persists longer EEs. plays pivotal role recruitment motor proteins subsequent movement Consistently, observed mediated alkalization hindered movement. Specifically, speed run-length were negatively impacted, ultimately leading falling off microtubules impairing delivery cargo LEs. thus offers unique opportunity viable therapeutic target impede cell entry.

Язык: Английский

Процитировано

0

Molecular basis for the assembly of the dynein transport machinery on microtubules DOI Creative Commons
Qinhui Rao, Pengxin Chai, Kai Zhang

и другие.

bioRxiv (Cold Spring Harbor Laboratory), Год журнала: 2024, Номер unknown

Опубликована: Дек. 30, 2024

Abstract Cytoplasmic dynein-1, a microtubule-based motor protein, requires dynactin and an adaptor to form the processive dynein-dynactin-adaptor (DDA) complex. The role of microtubules in DDA assembly has been elusive. Here, we reveal detailed structural insights into microtubule-mediated using cryo-electron microscopy. We find that adaptor-independent dynein- complex (DD) predominantly forms on intrinsic 2:1 stoichiometry, induced by spontaneous parallelization dynein upon microtubule binding. Adaptors can squeeze exchange within assembled microtubule-bound DD complex, which is enabled relative rotations between dynactin, further facilitated light intermediate chains assist ‘search’ mechanism. Our findings elucidate dynamic adaptability transport machinery, new mode for motile

Язык: Английский

Процитировано

0