Janusein and EB Cooperate to Enhance Microtubule Plus-end Catastrophe
- 1Tsinghua University
Abstract
Microtubule (MT) plus ends are organized by end-binding (EB) proteins, yet how EB-associated factors modulate the transition from growth to catastrophe remains incompletely understood. Using spatially resolved proximity proteomics, we identified Janusein (ZC2HC1A) as a conserved, poorly characterized MT-associated protein (MAP). At low expression levels, Janusein tracked MT plus ends and reduced EB comet velocity; at higher levels, it redistributed to the MT lattice and was associated with MT bundling and widespread MT loss. Loss of Janusein resulted in spindle defects in human cells. In vitro, Janusein alone facilitated MT elongation through its C-terminal fragment, but promoted MT catastrophe through its N-terminal fragment in the presence of EB proteins. Molecular dynamics simulations and mutational analyses suggest that an N-terminal loop may perturb lateral contacts between adjacent MT protofilaments. Together, these findings identify Janusein as an unconventional MAP that functionally cooperates with EB proteins to promote MT catastrophe.
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BibTeX
@misc{xu2026janusein,
title = {{Janusein and EB Cooperate to Enhance Microtubule Plus-end Catastrophe}},
author = {K. Xu and Z. Guo and Y. Cao and Y. Ye and C. Guan and K. Jiang and W. Li and G. Ou},
howpublished = {bioRxiv},
year = {2026},
month = oct,
doi = {10.64898/2026.10.26.761828},
url = {https://www.biorxiv.org/content/10.64898/2026.10.26.761828v1},
note = {CC BY-NC},
}
RIS
TY - UNPB
TI - Janusein and EB Cooperate to Enhance Microtubule Plus-end Catastrophe
AU - K. Xu
AU - Z. Guo
AU - Y. Cao
AU - Y. Ye
AU - C. Guan
AU - K. Jiang
AU - W. Li
AU - G. Ou
PY - 2026
DA - 2026/10/26
PB - bioRxiv
DO - 10.64898/2026.10.26.761828
UR - https://www.biorxiv.org/content/10.64898/2026.10.26.761828v1
AB - Microtubule (MT) plus ends are organized by end-binding (EB) proteins, yet how EB-associated factors modulate the transition from growth to catastrophe remains incompletely understood. Using spatially resolved proximity proteomics, we identified Janusein (ZC2HC1A) as a conserved, poorly characterized MT-associated protein (MAP). At low expression levels, Janusein tracked MT plus ends and reduced EB comet velocity; at higher levels, it redistributed to the MT lattice and was associated with MT bundling and widespread MT loss. Loss of Janusein resulted in spindle defects in human cells. In vitro, Janusein alone facilitated MT elongation through its C-terminal fragment, but promoted MT catastrophe through its N-terminal fragment in the presence of EB proteins. Molecular dynamics simulations and mutational analyses suggest that an N-terminal loop may perturb lateral contacts between adjacent MT protofilaments. Together, these findings identify Janusein as an unconventional MAP that functionally cooperates with EB proteins to promote MT catastrophe.
ER -