An NSF-like ATPase, p97, and NSF mediate cisternal regrowth from mitotic Golgi fragments

Article Abstract:

The inhibition of the growth of cisternae in mitotic Golgi fragments by the action of N-ethylmalemide (NEM) or salt washing can be removed by the addition of p97, a NEM-sensitive factor (NSF) -like ATPase or NSF along with SNAPs and the protein p115. Although the cistern in the cell-free systems grow, stacking does not take place. The cisternae formed by growth in the presence of NSF-SNAPs-p115 have dilated rims associated with a cluster of vescicles and are fenestrated as compared to those grown in the presence of p97.

Physiological aspects, Observations, Membrane fusion, Adenosine triphosphatase

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Cdc2 kinase directly phosphorylates the cis-Golgi matrix protein GM130 and is required for Golgi fragmentation in mitosis

Article Abstract:

GM130 can be directly phosphorylated by Cdc2 kinase. It has also been possible to produce evidence to show that Cdc2 activity is vital for mitotic Golgi fragmentation, while MEK1 is not vital for this process either in vitro or in vivo. The low MEK1 activity in mitosis is consistent with MEK1 not being a key mitotic regulator of Golgi fragmentation. Inhibition of MEK1 with PD, depletion of MEK1 or addition of active MEK1 has no impact on GM130 phosphorylation or Golgi fragmentation.

Cell cycle

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Syntaxin 5 is a common component of the NSF-and p97-mediated reassembly pathways of Golgi cisternae from mitotic Golgi fragments in vitro

Article Abstract:

Research was conducted to test whether syntaxin 5 act as a common component of the fusion pathways that rebuild Golgi cisternae from mitotic Golgi fragments. Proteins were fractionated by SDS-PAGe and then transferred to nitrocellulose while several forms of recombinant syntaxin 5 were determined by compromising the cytoplasmic domain. Results indicated a role for the p47 cofactor on the p97 pathway and showed that p97/947 exists as a stable cytosolic complex.

Analysis, Mitosis, Cell physiology

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