Biomaterial Database

Unlocking the mysteries of Na+-K+-ATPase endocytosis: phosphorylation is the key. 2006

James F Collawn

UI	MeSH Term	Description	Entries
D010766	Phosphorylation	The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.	Phosphorylations
D004705	Endocytosis	Cellular uptake of extracellular materials within membrane-limited vacuoles or microvesicles. ENDOSOMES play a central role in endocytosis.	Endocytoses
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000254	Sodium-Potassium-Exchanging ATPase	An enzyme that catalyzes the active transport system of sodium and potassium ions across the cell wall. Sodium and potassium ions are closely coupled with membrane ATPase which undergoes phosphorylation and dephosphorylation, thereby providing energy for transport of these ions against concentration gradients.	ATPase, Sodium, Potassium,Adenosinetriphosphatase, Sodium, Potassium,Na(+)-K(+)-Exchanging ATPase,Na(+)-K(+)-Transporting ATPase,Potassium Pump,Sodium Pump,Sodium, Potassium ATPase,Sodium, Potassium Adenosinetriphosphatase,Sodium-Potassium Pump,Adenosine Triphosphatase, Sodium, Potassium,Na(+) K(+)-Transporting ATPase,Sodium, Potassium Adenosine Triphosphatase,ATPase Sodium, Potassium,ATPase, Sodium-Potassium-Exchanging,Adenosinetriphosphatase Sodium, Potassium,Pump, Potassium,Pump, Sodium,Pump, Sodium-Potassium,Sodium Potassium Exchanging ATPase,Sodium Potassium Pump
D017346	Protein Serine-Threonine Kinases	A group of enzymes that catalyzes the phosphorylation of serine or threonine residues in proteins, with ATP or other nucleotides as phosphate donors.	Protein-Serine-Threonine Kinases,Serine-Threonine Protein Kinase,Serine-Threonine Protein Kinases,Protein-Serine Kinase,Protein-Serine-Threonine Kinase,Protein-Threonine Kinase,Serine Kinase,Serine-Threonine Kinase,Serine-Threonine Kinases,Threonine Kinase,Kinase, Protein-Serine,Kinase, Protein-Serine-Threonine,Kinase, Protein-Threonine,Kinase, Serine-Threonine,Kinases, Protein Serine-Threonine,Kinases, Protein-Serine-Threonine,Kinases, Serine-Threonine,Protein Kinase, Serine-Threonine,Protein Kinases, Serine-Threonine,Protein Serine Kinase,Protein Serine Threonine Kinase,Protein Serine Threonine Kinases,Protein Threonine Kinase,Serine Threonine Kinase,Serine Threonine Kinases,Serine Threonine Protein Kinase,Serine Threonine Protein Kinases
D033962	Adaptor Protein Complex 2	An adaptor protein complex primarily involved in the formation of clathrin-related endocytotic vesicles (ENDOSOMES) at the CELL MEMBRANE.	Clathrin Adaptor Protein Complex 2,Clathrin Assembly Protein Complex 2,AP-2 Adaptor (Clathrin-Coated Vesicles),AP-2 Protein Complex,Adaptor-Related Protein Complex 2,HA-2 Adaptors,Hydroxyapatite 2 Adaptors,AP 2 Protein Complex,Adaptor Related Protein Complex 2,HA 2 Adaptors

Related Publications

James F Collawn

Phosphorylation and ubiquitination are necessary for Na,K-ATPase endocytosis during hypoxia.

September 2007, Cellular signalling,

James F Collawn

Phosphorylation of the Na+,K+-ATPase and the H+,K+-ATPase.

June 2010, FEBS letters,

James F Collawn

Unlocking mysteries of gut sensory transmission: is adenosine the key?

October 2001, News in physiological sciences : an international journal of physiology produced jointly by the International Union of Physiological Sciences and the American Physiological Society,

James F Collawn

Phosphorylation of the catalyic alpha-subunit constitutes a triggering signal for Na+,K+-ATPase endocytosis.

April 1998, The Journal of biological chemistry,

James F Collawn

Phosphorylation of H2O2-treated lens Na+,K+-ATPase.

October 1984, Experimental eye research,

James F Collawn

[Phosphorylation of Na+, K+-ATPase--ion transport mechanism].

September 1983, Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme,

James F Collawn

Ouabain-induced endocytosis and signal transduction of the Na/K-ATPase.

September 2005, Frontiers in bioscience : a journal and virtual library,