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The Mother Centriole Appendage Protein Cenexin Modulates Lumen Formation through
Spindle Orientation
#MMPMID26948879
Hung HF
; Hehnly H
; Doxsey S
Curr Biol
2016[Mar]; 26
(6
): 793-801
PMID26948879
show ga
Establishing apical-basal polarity is instrumental in the functional shaping of a
solitary lumen within an acinus. By exploiting micropatterned slides, wound
healing assays, and three-dimensional culture systems, we identified a mother
centriole subdistal appendage protein, cenexin, as a critical player in symmetric
lumen expansion through the control of microtubule organization. In this regard,
cenexin was required for both centrosome positioning in interphase cells and
proper spindle orientation during mitosis. In contrast, the essential mother
centriole distal appendage protein CEP164 did not play a role in either process,
demonstrating the specificity of subdistal appendages for these events.
Importantly, upon closer examination we found that cenexin depletion decreased
astral microtubule length, disrupted astral microtubule minus-end organization,
and increased levels of the polarity protein NuMA at the cell cortex.
Interestingly, spindle misorientation and NuMA mislocalization were reversed by
treatment with a low dose of the microtubule-stabilizing agent paclitaxel. Taken
together, these results suggest that cenexin modulates microtubule organization
and stability to mediate spindle orientation.
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