Spatiotemporal Interactions of Myristoylated Alanine-Rich C Kinase Substrate (MARCKS) Protein with the Actin Cytoskeleton and Exocytosis of Oxytocin upon Prostaglandin F2α Stimulation of Bovine Luteal Cells1
Author:
Publisher
Oxford University Press (OUP)
Subject
Cell Biology,General Medicine,Reproductive Medicine
Link
http://academic.oup.com/biolreprod/article-pdf/69/6/2053/10590809/biolreprod2053.pdf
Reference24 articles.
1. Luteal neurophysin in the nonpregnant cow and ewe: immunocytochemical localization in membrane-bound secretory granules of the large luteal cell.;Endocrinology,1986
2. Ultrastructural localization of oxytocin and neurophysin in the ovine corpus luteum.;Cell Tissue Res,1986
3. Regulation by phosphorylation of reversible association of a myristoylated protein kinase C substrate with the plasma membrane.;Nature,1991
4. MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium-calmodulin.;Nature,1992
5. Phosphorylation-regulated calmodulin binding to a prominent cellular substrate for protein kinase C.;J Biol Chem,1989
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1. MARCKS and Lung Disease;American Journal of Respiratory Cell and Molecular Biology;2019-01
2. MARCKS phosphorylation and amylase release in GLP-1-stimulated acini isolated from rat pancreas;The Journal of Physiological Sciences;2018-05-29
3. Vías implicadas en la luteólisis bovina;Revista Colombiana de Ciencias Pecuarias;2016-07-22
4. Involvement of myristoylated alanine-rich C kinase substrate phosphorylation and translocation in cholecystokinin-induced amylase release in rat pancreatic acini;AM J PHYSIOL-GASTR L;2016
5. In Vitro Neutrophil Migration Requires Protein Kinase C-Delta (δ-PKC)-Mediated Myristoylated Alanine-Rich C-Kinase Substrate (MARCKS) Phosphorylation;Inflammation;2014-12-17
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