A compound membranous cytoplasmic organelle of eukaryotic cells, consisting of flattened, ribosome-free vesicles arranged in a more or less regular stack. The Golgi apparatus differs from the endoplasmic reticulum in often having slightly thicker membranes, appearing in sections as a characteristic shallow semicircle so that the convex side (cis or entry face) abuts the endoplasmic reticulum, secretory vesicles emerging from the concave side (trans or exit face). In vertebrate cells there is usually one such organelle, while in invertebrates and plants, where they are known usually as dictyosomes, there may be several scattered in the cytoplasm. The Golgi apparatus processes proteins produced on the ribosomes of the rough endoplasmic reticulum; such processing includes modification of the core oligosaccharides of glycoproteins, and the sorting and packaging of proteins for transport to a variety of cellular locations. Three different regions of the Golgi are now recognized both in terms of structure and function: cis, in the vicinity of the cis face, trans, in the vicinity of the trans face, and medial, lying between the cis and trans regions.

The set of thin, flattened membrane-bounded compartments, called cisternae, that form the central portion of the Golgi complex. The stack usually comprises cis, medial, and trans cisternae; the cis- and trans-Golgi networks are not considered part of the stack.

Catalysis of the reaction: heparosan-N-sulfate D-glucuronate = heparosan-N-sulfate L-iduronate.

The volume enclosed by the membranes of any cisterna of the Golgi apparatus.

The middle Golgi cisterna (or cisternae).

Any vesicle associated with the Golgi complex and involved in mediating transport within the Golgi or between the Golgi and other parts of the cell.

Cell death resulting from activation of endogenous cellular processes, by a mechanism other than apoptosis.

hyperphosphorylation of RNA polymerase II

CTD domain phosphorylation of RNA polymerase II

The production of an RNA polymerase II enzyme where the C-Terminal Domain (CTD) of the largest subunit is extensively phosphorylated, as a result of activation of kinases, deactivation of phosphatases, or both. This phosphorylation occurs during the initiation phase and is required for the transition to the elongation phase. Specific types of phosphorylation within the CTD are associated with recruitment of complexes such as the capping enzyme or 3'-RNA processing machinery to the elongating RNA polymerase complex.