Abstract
CD44 is a universally and abundantly expressed single-pass type I protein that spans the cytoplasmic membrane and is considered the principal receptor for hyaluronan in the extracellular matrix. CD44 exerts a multitude of biological functions, especially in cell adhesion and migration, and its deregulation has several pathological implications, including a putative role in cancer cell dissemination. Here we report the NMR chemical shift assignment of the recombinant intrinsically disordered CD44 cytoplasmic region (669–742).
Highlights
CD44 is the principal transmembrane receptor of the glycosaminoglycan hyaluronan (HA), which can be found in abundance in the extracellular matrix (Toole 2004)
We present the NMR assignment of the CD44 cytoplasmic tail generated after γ-secretase cleavage of full-length CD44
Cells were lysed via sonication, followed by centrifugation at 18,000 rpm and 4 °C for 40 min after which the supernatant was heated to 80 °C for 10 min to facilitate precipitation of heat-sensitive impurities which were separated from the sample by subsequent centrifugation at 18,000 rpm and 4 °C for 40 min
Summary
CD44 is the principal transmembrane receptor of the glycosaminoglycan hyaluronan (HA), which can be found in abundance in the extracellular matrix (Toole 2004). CD44, has attracted particular interest due to its prominent role in several pathologies, especially in the context of cancer initiation and metastasis (Naor et al 2009; Zöller 2011; Goldman et al 2015; Wang et al 2018) It was discovered early on, that the functionality of the receptor is influenced by post translational modifications that target the intrinsically disordered C-terminal region of the protein, that is found on the cytoplasmic side of the cell.
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
