In this study, we identified a rare CRY2 variant, p.Ser420Phe
First-pass extracted concept
CRY2 p.Ser420Phe variant
Candidate: toolkit item1 source documents6 linked claims
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Aliases
CRY2 variant p.Ser420Phe, p.Ser420Phe CRY2
Evidence Snippets
Supporting Sources
Linked Claims
Wild-type CRY2 and the CRY2 variant are degraded by a lysosomal-mediated degradation pathway.
Quoted textsource-backed
Further studies revealed that wild-type and CRY2 variants are degraded by the lysosomal-mediated degradation pathway, a mechanism not previously associated with CRY2.
The CRY2 p.Ser420Phe variant has reduced repression activity on CLOCK:BMAL1-driven transcription.
Quoted textsource-backed
Functional characterization of this variant at the cellular level revealed that p.Ser420Phe CRY2 had reduced repression activity on CLOCK:BMAL1-driven transcription
Ser-420 of CRY2 is required for interaction with the E3 ligases FBXL3 and FBXL21.
Quoted textsource-backed
which suggests Ser-420 of CRY2 is required for the interaction with E3 ligases
The CRY2 p.Ser420Phe variant is resistant to canonical proteasomal degradation because it loses interactions with the E3 ligases FBXL3 and FBXL21.
Quoted textsource-backed
the CRY2 variant exhibited an unexpected resistance to degradation via the canonical proteasomal pathway, primarily due to the loss of interactions with E3 ligases (FBXL3 and FBXL21)
The reduced repression activity of CRY2 p.Ser420Phe is due to reduced affinity for PER2 and defective nuclear translocation.
Quoted textsource-backed
due to its reduced affinity to the core clock protein PER2 and defective translocation into the nucleus
In Cry1-/-Cry2-/- double knockout mouse embryonic fibroblasts, complementation with the CRY2 p.Ser420Phe variant causes a 7 h shorter circadian period length.
Quoted textsource-backed
our complementation study with Cry1-/-Cry2-/- double knockout mouse embryonic fibroblast cells indicated that the CRY2 variant caused a 7 h shorter circadian period length