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Cortical Num1p interacts with the dynein intermediate chain Pac11p and cytoplasmic microtubules in budding yeast.

Farkasovsky M, Küntzel H - J. Cell Biol. (2001)

Bottom Line: The bud tip location of Num1p depends on Bni1p but does not require Kar9p, Dyn1p, or cMTs, whereas cMT contacts with polar Num1p dots are reduced in cells lacking Dyn1p.Num1p also forms a complex with Bni1p and Kar9p, although Num1p is not required for Bni1p- and Kar9p-dependent nuclear migration to the bud neck in preanaphase cells.In addition, Num1p may transiently cooperate with an associated Bni1p-Kar9p complex at the bud tip of early anaphase cells.

View Article: PubMed Central - PubMed

Affiliation: Max-Planck Institute for Experimental Medicine, D-37075 Göttingen, Germany.

ABSTRACT
Num1p, a cortical 313-kD protein, controls cytoplasmic microtubule (cMT) functions and nuclear migration through the bud neck in anaphase cells. A green fluorescent protein (GFP)-Num1p fusion protein localizes at the bud tip and the distal mother pole of living cells, apparently forming cMT capture sites at late anaphase. In addition, galactose-induced GFP-Num1p is seen at the bud neck and in lateral regions of the mother cortex. The bud tip location of Num1p depends on Bni1p but does not require Kar9p, Dyn1p, or cMTs, whereas cMT contacts with polar Num1p dots are reduced in cells lacking Dyn1p. Num1p associates with the dynein intermediate chain Pac11p in the presence of Dyn1p, and with the alpha-tubulin Tub3p, as shown by coimmune precipitation of tagged proteins. Num1p also forms a complex with Bni1p and Kar9p, although Num1p is not required for Bni1p- and Kar9p-dependent nuclear migration to the bud neck in preanaphase cells. Our data suggest that Num1p controls nuclear migration during late anaphase by forming dynein-interacting cortical cMT capture sites at both cellular poles. In addition, Num1p may transiently cooperate with an associated Bni1p-Kar9p complex at the bud tip of early anaphase cells.

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Quantification of cell cycle–dependent localization of galactose-induced GFP-Num1p. 200–250 cells (FMY519) of different stages, as determined by nuclear and microtubule positions, were scored for prominent cortical dot positions at cellular poles and bud neck sites. Additional dots at the mother cortex are not depicted.
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Figure 3: Quantification of cell cycle–dependent localization of galactose-induced GFP-Num1p. 200–250 cells (FMY519) of different stages, as determined by nuclear and microtubule positions, were scored for prominent cortical dot positions at cellular poles and bud neck sites. Additional dots at the mother cortex are not depicted.

Mentions: Fig. 3 summarizes the appearance of prominent galactose-induced GFP-Num1p dots in cells of various cell cycle stages (less prominent dots at the mother cortex are not depicted). Two opposite Num1p dots are seen in 96% of G1 cells; one of the two dots is close to the incipient bud site and appears to persist at the mother side of the neck through S, G2, and M phase. The tip of the growing bud is marked by a Num1p dot at S/G2 and persists through mitosis.


Cortical Num1p interacts with the dynein intermediate chain Pac11p and cytoplasmic microtubules in budding yeast.

Farkasovsky M, Küntzel H - J. Cell Biol. (2001)

Quantification of cell cycle–dependent localization of galactose-induced GFP-Num1p. 200–250 cells (FMY519) of different stages, as determined by nuclear and microtubule positions, were scored for prominent cortical dot positions at cellular poles and bud neck sites. Additional dots at the mother cortex are not depicted.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2199608&req=5

Figure 3: Quantification of cell cycle–dependent localization of galactose-induced GFP-Num1p. 200–250 cells (FMY519) of different stages, as determined by nuclear and microtubule positions, were scored for prominent cortical dot positions at cellular poles and bud neck sites. Additional dots at the mother cortex are not depicted.
Mentions: Fig. 3 summarizes the appearance of prominent galactose-induced GFP-Num1p dots in cells of various cell cycle stages (less prominent dots at the mother cortex are not depicted). Two opposite Num1p dots are seen in 96% of G1 cells; one of the two dots is close to the incipient bud site and appears to persist at the mother side of the neck through S, G2, and M phase. The tip of the growing bud is marked by a Num1p dot at S/G2 and persists through mitosis.

Bottom Line: The bud tip location of Num1p depends on Bni1p but does not require Kar9p, Dyn1p, or cMTs, whereas cMT contacts with polar Num1p dots are reduced in cells lacking Dyn1p.Num1p also forms a complex with Bni1p and Kar9p, although Num1p is not required for Bni1p- and Kar9p-dependent nuclear migration to the bud neck in preanaphase cells.In addition, Num1p may transiently cooperate with an associated Bni1p-Kar9p complex at the bud tip of early anaphase cells.

View Article: PubMed Central - PubMed

Affiliation: Max-Planck Institute for Experimental Medicine, D-37075 Göttingen, Germany.

ABSTRACT
Num1p, a cortical 313-kD protein, controls cytoplasmic microtubule (cMT) functions and nuclear migration through the bud neck in anaphase cells. A green fluorescent protein (GFP)-Num1p fusion protein localizes at the bud tip and the distal mother pole of living cells, apparently forming cMT capture sites at late anaphase. In addition, galactose-induced GFP-Num1p is seen at the bud neck and in lateral regions of the mother cortex. The bud tip location of Num1p depends on Bni1p but does not require Kar9p, Dyn1p, or cMTs, whereas cMT contacts with polar Num1p dots are reduced in cells lacking Dyn1p. Num1p associates with the dynein intermediate chain Pac11p in the presence of Dyn1p, and with the alpha-tubulin Tub3p, as shown by coimmune precipitation of tagged proteins. Num1p also forms a complex with Bni1p and Kar9p, although Num1p is not required for Bni1p- and Kar9p-dependent nuclear migration to the bud neck in preanaphase cells. Our data suggest that Num1p controls nuclear migration during late anaphase by forming dynein-interacting cortical cMT capture sites at both cellular poles. In addition, Num1p may transiently cooperate with an associated Bni1p-Kar9p complex at the bud tip of early anaphase cells.

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