The sialidase NEU1 directly interacts with the juxtamembranous segment of the cytoplasmic domain of mucin-1 to inhibit downstream PI3K-Akt signaling

The extracellular domain (ED) of the membrane-spanning sialoglycoprotein, mucin-1 (MUC1), is an in vivo substrate for the lysosomal sialidase, neuraminidase-1 (NEU1). Engagement of the MUC1-ED by its cognate ligand, Pseudomonas aeruginosa-expressed flagellin, increases NEU1-MUC1 association and NEU1...

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Veröffentlicht in:	The Journal of biological chemistry 2021-11, Vol.297 (5), p.101337-101337, Article 101337
Hauptverfasser:	Hyun, Sang W., Imamura, Akihiro, Ishida, Hideharu, Piepenbrink, Kurt H., Goldblum, Simeon E., Lillehoj, Erik P.
Format:	Artikel
Sprache:	eng
Schlagworte:	A549 Cells Akt PBK Amino Acid Substitution cell surface associated (MUC1) HEK293 Cells Humans mucin 1 Mucin-1 - genetics Mucin-1 - metabolism Mutation, Missense Neuraminidase - genetics Neuraminidase - metabolism neuraminidase-1 phosphatidylinositide 3-kinase (PI 3-kinase) Phosphatidylinositol 3-Kinases - genetics Phosphatidylinositol 3-Kinases - metabolism Protein Domains Proto-Oncogene Proteins c-akt - genetics Proto-Oncogene Proteins c-akt - metabolism sialic acid sialidase Signal Transduction
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