🎄 xmas preprint 🎄 we are excited to share our cryo-EM structure of UBR4 in complex with KCMF1 and CALM1. the PQC ligase forms a massive ubiquitination arena, primed to amplify ubiquitin chains (E4 activity) and boost degradation of defective proteins. www.biorxiv.org/content/10.1...
December 21, 2024 at 10:46 AM
🎄 xmas preprint 🎄 we are excited to share our cryo-EM structure of UBR4 in complex with KCMF1 and CALM1. the PQC ligase forms a massive ubiquitination arena, primed to amplify ubiquitin chains (E4 activity) and boost degradation of defective proteins. www.biorxiv.org/content/10.1...
Structural and mechanistic insights into the UBR4-KCMF1-Calmodulin complex @ispt-proteinterm.bsky.social academic.oup.com/proteincell/...
Structural and mechanistic insights into the UBR4-KCMF1-Calmodulin complex
Dear Editor,
academic.oup.com
June 23, 2026 at 9:20 AM
Structural and mechanistic insights into the UBR4-KCMF1-Calmodulin complex @ispt-proteinterm.bsky.social academic.oup.com/proteincell/...
How to define degrons and E3 ligase specificities by peptide pulldowns | Methods in Enzymology | Kwon and Ji labs | #KCMF1 #Cysteine #Arg/N-degron @ispt-proteinterm.bsky.social www.sciencedirect.com/science/arti...
August 7, 2025 at 7:11 AM
How to define degrons and E3 ligase specificities by peptide pulldowns | Methods in Enzymology | Kwon and Ji labs | #KCMF1 #Cysteine #Arg/N-degron @ispt-proteinterm.bsky.social www.sciencedirect.com/science/arti...
Coenzyme A biosynthesis is regulated by two distinct Ubiquitin E3 ligase complexes | UBR4-KCMF1 and MKLN1-CTLH independently converge on a common N-terminal MK Arg/N-degron to promote PANK degradation and restrict CoA biosynthesis | @ispt-proteinterm.bsky.social www.biorxiv.org/content/10.6...
Parallel Arg/N-degron recognition systems regulate coenzyme A biosynthesis
Coenzyme A (CoA) is an essential metabolic cofactor whose biosynthesis is controlled by pantothenate kinases (PANKs), the rate-limiting enzymes in CoA synthesis. Although CoA production is extensively...
www.biorxiv.org
September 21, 2026 at 7:44 AM
Coenzyme A biosynthesis is regulated by two distinct Ubiquitin E3 ligase complexes | UBR4-KCMF1 and MKLN1-CTLH independently converge on a common N-terminal MK Arg/N-degron to promote PANK degradation and restrict CoA biosynthesis | @ispt-proteinterm.bsky.social www.biorxiv.org/content/10.6...
SIFI transfers the first ubiquitin to substrates with help from its KCMF1 subunit, which is located within a highly flexible part of the structure that can adapt its conformation to distinct substrates.
December 3, 2024 at 7:05 AM
SIFI transfers the first ubiquitin to substrates with help from its KCMF1 subunit, which is located within a highly flexible part of the structure that can adapt its conformation to distinct substrates.
Another mega E3 ligase with intriguing structural insights
Structure highlighting the targeting of a myriad of possible substrates by UBR4 alongside KCMF1 co-factor (not E3 ligase in my view for many years)
#ubiquitin #science #literature #biology
Structure highlighting the targeting of a myriad of possible substrates by UBR4 alongside KCMF1 co-factor (not E3 ligase in my view for many years)
#ubiquitin #science #literature #biology
🎄 xmas preprint 🎄 we are excited to share our cryo-EM structure of UBR4 in complex with KCMF1 and CALM1. the PQC ligase forms a massive ubiquitination arena, primed to amplify ubiquitin chains (E4 activity) and boost degradation of defective proteins. www.biorxiv.org/content/10.1...
January 23, 2025 at 12:11 PM
Another mega E3 ligase with intriguing structural insights
Structure highlighting the targeting of a myriad of possible substrates by UBR4 alongside KCMF1 co-factor (not E3 ligase in my view for many years)
#ubiquitin #science #literature #biology
Structure highlighting the targeting of a myriad of possible substrates by UBR4 alongside KCMF1 co-factor (not E3 ligase in my view for many years)
#ubiquitin #science #literature #biology
はぐれタンパク質を分解する
複合体を組めなかったりした"はぐれタンパク質"は適切に分解される必要がある。今回レポーターや質量分析を用いて、この分解に重要な因子を同定(UBR4-KCMF1 )。複数の経路がUBR4-KCMF1に収束するらしい
複合体の品質管理面白い
複合体を組めなかったりした"はぐれタンパク質"は適切に分解される必要がある。今回レポーターや質量分析を用いて、この分解に重要な因子を同定(UBR4-KCMF1 )。複数の経路がUBR4-KCMF1に収束するらしい
複合体の品質管理面白い
www.cell.com
January 29, 2025 at 10:00 AM
はぐれタンパク質を分解する
複合体を組めなかったりした"はぐれタンパク質"は適切に分解される必要がある。今回レポーターや質量分析を用いて、この分解に重要な因子を同定(UBR4-KCMF1 )。複数の経路がUBR4-KCMF1に収束するらしい
複合体の品質管理面白い
複合体を組めなかったりした"はぐれタンパク質"は適切に分解される必要がある。今回レポーターや質量分析を用いて、この分解に重要な因子を同定(UBR4-KCMF1 )。複数の経路がUBR4-KCMF1に収束するらしい
複合体の品質管理面白い
We found that NatC acetylation can shield proteins from degradation via the Arg/N-degron pathway through UBR4-KCMF1. (See Varland et al, 2023 Nature Communications www.nature.com/articles/s41...
N-terminal acetylation shields proteins from degradation and promotes age-dependent motility and longevity - Nature Communications
The most common protein modification in eukaryotes is N-terminal acetylation, but its functional impact has remained enigmatic. Here, the authors find that a key role for N-terminal acetylation is shi...
www.nature.com
April 28, 2026 at 8:43 AM
We found that NatC acetylation can shield proteins from degradation via the Arg/N-degron pathway through UBR4-KCMF1. (See Varland et al, 2023 Nature Communications www.nature.com/articles/s41...
Potassium channel modulatory factor 1 (KCMF1:p) sounds like a great name, except it is an E3 ubiquitin ligase & part of the N-rule pathway. It features an N-terminal lit S2+phosphoryl acceptor & a major phosphoIDR between the nward zinc finger domains & the most nward of 2 helical patches.
March 24, 2025 at 11:47 AM
Potassium channel modulatory factor 1 (KCMF1:p) sounds like a great name, except it is an E3 ubiquitin ligase & part of the N-rule pathway. It features an N-terminal lit S2+phosphoryl acceptor & a major phosphoIDR between the nward zinc finger domains & the most nward of 2 helical patches.
Potassium channel modulatory factor 1 (KCMF1:p) sounds like a great name, except it is an E3 ubiquitin ligase & part of the N-rule pathway. It features an N-terminal lit S2+phosphoryl acceptor & a major phosphoIDR between the nward zinc finger domains & the most nward of 2 helical patches.
March 24, 2025 at 11:49 AM
Potassium channel modulatory factor 1 (KCMF1:p) sounds like a great name, except it is an E3 ubiquitin ligase & part of the N-rule pathway. It features an N-terminal lit S2+phosphoryl acceptor & a major phosphoIDR between the nward zinc finger domains & the most nward of 2 helical patches.