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Vol. 20, Issue 20, 4335-4347, October 15, 2009

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Organization and Dynamics of the Aspergillus nidulans Golgi during Apical Extension and Mitosis

Departamento de Microbiología Molecular, Centro de Investigaciones Biológicas C.S.I.C., Madrid 28040, Spain

Submitted March 30, 2009; Revised July 31, 2009; Accepted August 11, 2009
Monitoring Editor: Sean Munro

Aspergillus nidulans hyphae grow exclusively by apical extension. Golgi equivalents (GEs) labeled with mRFP-tagged PH^OSBP domain form a markedly polarized, dynamic network of ring-shaped and fenestrated cisternae that remains intact during "closed" mitosis. mRFP-PH^OSBP GEs advance associated with the growing apex where secretion predominates but do not undergo long-distance movement toward the tip that could account for their polarization. mRFP-PH^OSBP GEs overlap with the trans-Golgi resident Sec7 but do not colocalize with also polarized accretions of the early Golgi marker GrhA^Grh1-GFP, indicating that early and late Golgi membranes segregate spatially. AnSec23-GFP ER exit sites (ERES) are numerous, relatively static foci localizing across the entire cell. However, their density is greatest near the tip, correlating with predominance of early and trans-Golgi elements in this region. Whereas GrhA-GFP structures and ERES reach the apical dome, mRFP-PH^OSBP GEs are excluded from this region, which contains the endosome dynein loading zone. After latrunculin-mediated F-actin disruption, mRFP-PH^OSBP GEs fragment and, like AnSec23-GFP ERES, depolarize. Brefeldin A transiently collapses late and early GEs into distinct aggregates containing Sec7/mRFP-PH^OSBP and GrhA-GFP, respectively, temporarily arresting apical extension. Rapid growth reinitiates after washout, correlating with reacquisition of the normal Golgi organization that, we conclude, is required for apical extension.

Address correspondence to: Miguel A. Peñalva (penalva{at}cib.csic.es).

Abbreviations used: BFA, brefeldin A; F-actin, filamentous polymers of actin; EM, electron microscopy; ER, endoplasmic reticulum; ERES, ER exit sites; GE, Golgi equivalent; GFP, green fluorescent protein; mRFP, monomeric red fluorescent protein; LatB, latrunculin B; MT(s), microtubule(s); NPCs, nuclear pore complexes; PH, pleckstrin homology domain; OSBP, human oxysterol binding protein; PLC, rat phospholipase 1; SPK, Spitzenkörper; UTR, untranslated region.

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