Protein fem-1 homolog A

Definition:

Substrate-recognition component of a Cul2-RING (CRL2) E3 ubiquitin-protein ligase complex of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation. The C-degron recognized by the DesCEND pathway is usually a motif of less than ten residues and can be present in full-length proteins, truncated proteins or proteolytically cleaved forms. The CRL2(FEM1A) complex specifically recognizes proteins with an arginine at the C-terminus: recognizes and binds proteins ending with -Lys/Arg-Xaa-Arg and -Lys/Arg-Xaa-Xaa-Arg C-degrons, such as SIL1 or OR51B2, leading to their ubiquitination and degradation. Promotes ubiquitination and degradation of SLBP. Involved in PGE2-EP4-mediated inhibition of inflammation of macrophages via interaction with NFKB1 and PTGER4 (By similarity). Promotes inflammation in brain microglia through MAP2K4/MKK4-mediated signaling (By similarity).

References:

[1]. John F Dankert, et al. FEM1 proteins are ancient regulators of SLBP degradation. Cell Cycle. 2017 Mar 19;16(6):556-564. [Content Brief]

[2]. Xiaojie Yan, et al. Molecular basis for ubiquitin ligase CRL2FEM1C-mediated recognition of C-degron. Nat Chem Biol. 2021 Mar;17(3):263-271. [Content Brief]

[3]. Xinyan Chen, et al. Molecular basis for arginine C-terminal degron recognition by Cul2FEM1 E3 ligase. Nat Chem Biol. 2021 Mar;17(3):254-262. [Content Brief]

[4]. Itay Koren, et al. The Eukaryotic Proteome Is Shaped by E3 Ubiquitin Ligases Targeting C-Terminal Degrons. Cell. 2018 Jun 14;173(7):1622-1635.e14. [Content Brief]

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