Live cell imaging of β-tubulin mRNA reveals spatiotemporal expression dynamics in the filamentous fungus Aspergillus oryzae DOI Creative Commons

Keishu Kawatomi,

Yuki Morita,

Yoshinori Katakura

et al.

Scientific Reports, Journal Year: 2024, Volume and Issue: 14(1)

Published: June 14, 2024

In filamentous fungi, microtubules are important for polar growth and morphological maintenance serve as rails intracellular trafficking. The molecular mechanisms associated with have been analyzed. However, little is known about when where tubulin, a component of microtubules, biosynthesized in multinuclear multicellular fungi. this study, we visualized based on the enhanced green fluorescence protein (EGFP)-labeled α-tubulin β-tubulin mRNA tagged by EGFP-mediated MS2 system living yellow Koji mold Aspergillus oryzae cells order to understand spatiotemporal production mechanism tubulin. We found that btuA, encoding β-tubulin, localized at dot-like structures through apical, middle basal regions hyphal cells. addition, some btuA dots showed microtubule-dependent motor protein-like dynamics Furthermore, it was were decreased cytoplasm just before mitosis but increased immediately after mitosis, followed gradual decrease. summary, localization abundance spatiotemporally regulated A.

Language: Английский

VezA/vezatin facilitates proper assembly of the dynactin complex in vivo DOI Open Access
Jun Zhang, Rongde Qiu,

Sean Xie

et al.

bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2024, Volume and Issue: unknown

Published: April 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.

Language: Английский

Citations

0
VezA/vezatin facilitates proper assembly of the dynactin complex in vivo DOI Creative Commons
Jun Zhang, Rongde Qiu,

Sean Xie

et al.

Cell Reports, Journal Year: 2024, Volume and Issue: 43(11), P. 114943 - 114943

Published: Nov. 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.

Language: Английский

Citations

0
VezA/Vezatin Facilitates Proper Assembly of the Dynactin Complex in vivo DOI
Jun Zhang, Rongde Qiu,

Sean Xie

et al.

Published: Jan. 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.

Language: Английский

Citations

0
Live cell imaging of β-tubulin mRNA reveals spatiotemporal expression dynamics in the filamentous fungus Aspergillus oryzae DOI Creative Commons

Keishu Kawatomi,

Yuki Morita,

Yoshinori Katakura

et al.

Scientific Reports, Journal Year: 2024, Volume and Issue: 14(1)

Published: June 14, 2024

In filamentous fungi, microtubules are important for polar growth and morphological maintenance serve as rails intracellular trafficking. The molecular mechanisms associated with have been analyzed. However, little is known about when where tubulin, a component of microtubules, biosynthesized in multinuclear multicellular fungi. this study, we visualized based on the enhanced green fluorescence protein (EGFP)-labeled α-tubulin β-tubulin mRNA tagged by EGFP-mediated MS2 system living yellow Koji mold Aspergillus oryzae cells order to understand spatiotemporal production mechanism tubulin. We found that btuA, encoding β-tubulin, localized at dot-like structures through apical, middle basal regions hyphal cells. addition, some btuA dots showed microtubule-dependent motor protein-like dynamics Furthermore, it was were decreased cytoplasm just before mitosis but increased immediately after mitosis, followed gradual decrease. summary, localization abundance spatiotemporally regulated A.

Language: Английский

Citations

0