@article {67844,
	title = {ER proteins decipher the tubulin code to regulate organelle distribution.},
	journal = {Nature},
	volume = {601},
	year = {2022},
	month = {2022 Jan 01},
	pages = {132-138},
	abstract = {<p>Organelles move along differentially modified microtubules to establish and maintain their proper distributions and functions. However, how cells interpret these post-translational microtubule modification codes to selectively regulate organelle positioning remains largely unknown. The endoplasmic reticulum\&nbsp;(ER) is an interconnected network of diverse morphologies that extends promiscuously throughout the cytoplasm, forming abundant contacts with other organelles. Dysregulation of endoplasmic reticulum morphology is tightly linked to neurologic disorders and cancer. Here we demonstrate that three membrane-bound endoplasmic reticulum proteins preferentially interact with different microtubule populations, with CLIMP63 binding centrosome microtubules, kinectin (KTN1) binding perinuclear polyglutamylated microtubules, and p180 binding glutamylated microtubules. Knockout of these proteins or manipulation of microtubule populations and glutamylation status results in marked changes in endoplasmic reticulum positioning, leading to similar redistributions of other organelles. During nutrient starvation, cells modulate CLIMP63 protein levels and p180-microtubule binding to bidirectionally move endoplasmic reticulum and lysosomes for proper autophagic responses.</p>
},
	issn = {1476-4687},
	doi = {10.1038/s41586-021-04204-9},
	author = {Zheng, Pengli and Obara, Christopher J and Szczesna, Ewa and Nixon-Abell, Jonathon and Mahalingan, Kishore K and Roll-Mecak, Antonina and Lippincott-Schwartz, Jennifer and Blackstone, Craig}
}
@article {49404,
	title = {Severing enzymes amplify microtubule arrays through lattice GTP-tubulin incorporation.},
	journal = {Science (New York, N.Y.)},
	volume = {361},
	year = {2018},
	month = {2018 Aug 24},
	abstract = {<p>Spastin and katanin sever and destabilize microtubules. Paradoxically, despite their destructive activity they increase microtubule mass in vivo. We combined single-molecule total internal reflection fluorescence microscopy and electron microscopy to show that the elemental step in microtubule severing is the generation of nanoscale damage throughout the microtubule by active extraction of tubulin heterodimers. These damage sites are repaired spontaneously by guanosine triphosphate (GTP)-tubulin incorporation, which rejuvenates and stabilizes the microtubule shaft. Consequently, spastin and katanin increase microtubule rescue rates. Furthermore, newly severed ends emerge with a high density of GTP-tubulin that protects them against depolymerization. The stabilization of the newly severed plus ends and the higher rescue frequency synergize to amplify microtubule number and mass. Thus, severing enzymes regulate microtubule architecture and dynamics by promoting GTP-tubulin incorporation within the microtubule shaft.</p>
},
	issn = {1095-9203},
	doi = {10.1126/science.aau1504},
	author = {Vemu, Annapurna and Szczesna, Ewa and Zehr, Elena A and Spector, Jeffrey O and Grigorieff, Nikolaus and Deaconescu, Alexandra M and Roll-Mecak, Antonina}
}
