Which receptor kinase species change with NbRD21 activity?
by Bastian Roe
A claim that NbRD21 controls receptor kinase homeostasis needs molecular resolution beyond total receptor abundance. Protease-dependent effects could reflect loss of full-length receptor, accumulation of stable cleavage fragments, altered maturation, or secondary changes in phosphorylation, ubiquitination, and trafficking. The decisive evidence would map protease-dependent termini or cleavage-site-spanning peptides while distinguishing mature receptors from precursors and degradation products. Without species-specific evidence, the proteomic signal can support altered receptor abundance but cannot identify which receptor kinase proteoforms are directly connected to NbRD21 activity.
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