Any process that stops, prevents or reduces the frequency, rate or extent of an iron transmembrane transporter activity.

OBSOLETE. Any process that modulates the frequency, rate or extent of the organization, biogenesis or maintenance of the cytoskeleton.

The modification of actin by addition of ubiquitin groups.

OBSOLETE. A cytoskeleton organization process that directly or indirectly links cytoskeletal filaments to the plasma membrane.

OBSOLETE. The resumption of the Saccharomyces mitotic cell division cycle by pheromone-arrested cells that have not mated.

OBSOLETE. The process of nucleolar expansion, as seen in Saccharomyces.

Establishment and formation of the optic placode, paired ectodermal placodes that become invaginated to form the embryonic lens vesicles.

A proton-transporting two-sector ATPase complex found in the lysosomal membrane, where it acts as a proton pump to mediate acidification of the lysosomal lumen.

A proton-transporting two-sector ATPase complex that couples ATP hydrolysis to the transport of protons across a concentration gradient. The resulting transmembrane electrochemical potential of H+ is used to drive a variety of (i) secondary active transport systems via H+-dependent symporters and antiporters and (ii) channel-mediated transport systems. The complex comprises a membrane sector (V0) that carries out proton transport and a cytoplasmic compartment sector (V1) that catalyzes ATP hydrolysis. V-type ATPases are found in the membranes of organelles such as vacuoles, endosomes, and lysosomes, and in the plasma membrane.

A proton-transporting two-sector ATPase complex found in the vacuolar membrane, where it acts as a proton pump to mediate acidification of the vacuolar lumen.

The V0 domain of a proton-transporting V-type ATPase found in the lysosomal membrane.

The V1 domain of a proton-transporting V-type ATPase found in the lysosomal membrane.

The aggregation and bonding together of alpha- and beta-tubulin to form a tubulin heterodimer.

The process in which tubulin alpha-beta heterodimers begin aggregation to form an oligomeric tubulin structure (a microtubule seed). Microtubule nucleation is the initiating step in the formation of a microtubule in the absence of any existing microtubules ('de novo' microtubule formation).

Completion of folding of alpha- and beta-tubulin; takes place subsequent to chaperonin-mediated partial folding; mediated by a complex of folding cofactors.