bioRxiv (Cold Spring Harbor Laboratory), Год журнала: 2023, Номер unknown
Опубликована: Апрель 18, 2023
Functions of protein SUMOylation remain incompletely understood in different cell types. The budding yeast machinery interacts with LIS1, a critical for dynein activation, but dynein-pathway components were not identified as SUMO-targets the filamentous fungus
Язык: Английский
bioRxiv (Cold Spring Harbor Laboratory), Год журнала: 2025, Номер unknown
Опубликована: Апрель 23, 2025
Motor-driven transport on microtubules is critical for distributing organelles throughout the cell. Most commonly, organelle movement mediated by cargo adaptors, proteins surface of an that directly recruit microtubule-based motors. An alternative mechanism called hitchhiking was recently discovered: some move, not recruiting motors directly, but instead using membrane contact sites to attach motor-driven vesicles and hitchhike along microtubules. Organelle observed across fungi animals. In filamentous fungi, nearly all peroxisomes move early endosomes (EEs). fungus Aspergillus nidulans , EE-associated linker PxdA DipA are establishing EE-peroxisome required peroxisome movement. How recognize this subset EEs what peroxisome-membrane exist can interact with known. Here, we undertook a forward mutagenesis screen identify such proteins. We discovered acyl-coA binding (ACB) domain-containing protein AcbdA/AN1062 localizes via its tail-anchored transmembrane domain (TMD). Deleting AcbdA gene or only N-terminal ACB perturbs distribution peroxisomes. Importantly, recruitment EEs. Fatty acid (FA)-induced increases in require AcbdA, suggesting coupled FA metabolism. Mutating conserved FFAT motif, predicted endoplasmic reticulum (ER), has no effect Taken together, our data indicate tether during hitchhiking. AcbdA’s involvement peroxisome-EE site formation represents divergence from known functions Acbd4/5 adds layers understanding functionality family
Язык: Английский
Процитировано
0
Genetics, Год журнала: 2023, Номер 225(4)
Опубликована: Сен. 19, 2023
Abstract Functions of protein SUMOylation remain incompletely understood in different cell types. Via forward genetics, here we identified ubaBQ247*, a loss-of-function mutation SUMO activation enzyme UbaB the filamentous fungus Aspergillus nidulans. The ΔubaB, and ΔsumO mutants all produce abnormal chromatin bridges, indicating importance completion chromosome segregation. bridges are enclosed by nuclear membrane containing peripheral pore complex proteins that normally get dispersed during mitosis, also surrounded cytoplasmic microtubules typical interphase cells. Time-lapse sequences further indicate most persist through prior to next anaphase segregation can new into interphase. When first mitosis happens at higher temperature 42°C, deficiency produces not only but many abnormally shaped single nuclei fail divide. UbaB-GFP localizes just like previously studied SumO-GFP, signals disappear when pores partially open, reappear after mitosis. localization is consistent with targets being proteins. Finally, although budding yeast machinery interacts LIS1, critical for dynein activation, loss does cause any obvious defect dynein-mediated transport early endosomes, unnecessary A.
Язык: Английский
Процитировано
2
bioRxiv (Cold Spring Harbor Laboratory), Год журнала: 2024, Номер unknown
Опубликована: Апрель 20, 2024
Abstract Cytoplasmic dynein-mediated intracellular transport needs the multi-component dynactin complex for cargo binding and motor activation. However, cellular factors involved in assembly remain unexplored. Here we found Aspergillus nidulans that vezatin homolog VezA is important assembly. affects microtubule plus-end accumulation of dynein before adapter-mediated activation, two processes both need dynactin. The contains multiple components including an Arp1 (actin-related protein 1) mini-filament associated with a pointed-end sub-complex. physically interacts either directly or indirectly via its Loss causes defect integrity, most likely by affecting connection between Using various mutants, further revealed must be highly coordinated. Together, these results shed new light on vivo.
Язык: Английский
Процитировано
0
Опубликована: Янв. 1, 2024
Cytoplasmic dynein-mediated intracellular transport needs the multi-component dynactin complex for cargo binding and motor activation. However, cellular factors involved in assembly remain unexplored. Here we found Aspergillus nidulans that vezatin homolog VezA is important assembly. affects microtubule plus-end accumulation of dynein before adapter-mediated activation, two processes both need dynactin. The contains multiple components including an Arp1 (actin-related protein 1) mini-filament associated with a pointed-end sub-complex. physically interacts either directly or indirectly via its Loss causes defect integrity, most likely by affecting connection between Using various mutants, further revealed must be highly coordinated. Together, these results shed new light on vivo.
Язык: Английский
Процитировано
0
Cell Reports, Год журнала: 2024, Номер 43(11), С. 114943 - 114943
Опубликована: Ноя. 1, 2024
Cytoplasmic dynein-mediated intracellular transport needs the multi-component dynactin complex for cargo binding and motor activation. However, cellular factors involved in assembly remain unexplored. Here, we found Aspergillus nidulans that vezatin homolog VezA is important assembly. affects microtubule plus-end accumulation of dynein before cargo-adapter-mediated activation, two processes both need dynactin. The contains multiple components, including p150, p50, an Arp1 (actin-related protein 1) mini-filament associated with a pointed-end sub-complex. physically interacts either directly or indirectly. Loss significantly decreases amount pulled down proteins, as well levels p50 p150 cell extract. Using various mutants, further revealed process must be highly coordinated. Together, these results shed light on vivo.
Язык: Английский
Процитировано
0
bioRxiv (Cold Spring Harbor Laboratory), Год журнала: 2023, Номер unknown
Опубликована: Апрель 18, 2023
Functions of protein SUMOylation remain incompletely understood in different cell types. The budding yeast machinery interacts with LIS1, a critical for dynein activation, but dynein-pathway components were not identified as SUMO-targets the filamentous fungus
Язык: Английский
Процитировано
0