Components of the JNK–MAPK pathway play distinct roles in hepatocellular carcinoma

Advances of E3 ligases in lung cancer

“…These E3 ligases exhibit a diversity in their structure and function; they can exist as single polypeptide chains or operate as part of larger protein complexes. Categorized based on their structural characteristics, E3 ubiquitin ligases can be divided into three notable families: HECT (homologous to E6-associated protein carboxyl terminus) family, RING (really interesting new gene) family and RBR (RING between RING-RING) family [ 19 ]. Each family member within these groups possesses unique functional attributes that set them apart, often due to the presence of specific protein interaction domains, as highlighted in.…”

“…The RING family is most typically characterized by ring finger domains, each of which is linked to two Zn 2+ ions. RING E3s rely on their ring finger domains to bind to E2s to function as E3s [ 19 ]. On this basis, due to the different structural domains, RING E3s can be divided into several subfamilies: The Membrane-associated RING-cysteine-histidine (MARCH) subfamily, protease-associated (PA)- multiple transmembrane (TM)-RING subfamily, tripartite motif (TRIM) subfamily and RING-Ub interacting motif (UIM) subfamily [ 21 ].…”

“…On this basis, due to the different structural domains, RING E3s can be divided into several subfamilies: The Membrane-associated RING-cysteine-histidine (MARCH) subfamily, protease-associated (PA)- multiple transmembrane (TM)-RING subfamily, tripartite motif (TRIM) subfamily and RING-Ub interacting motif (UIM) subfamily [ 21 ]. In addition, based on the form in which it functions, RING E3 ligases can be further categorized into monomeric RING, homodimeric RING, heterodimeric RING, cullin-RING (CRLs), and other multisubunit RING [ 19 ].…”

Ubiquitin specific peptidase 3: an emerging deubiquitinase that regulates physiology and diseases

“…Ubiquitin attaches covalently to lysine residues on the substrate through a series of enzymatic reactions involving ubiquitin-activating (E1s), ubiquitin-conjugating (E2s), and ubiquitin ligase (E3s) enzymes [3][4][5], resulting in mono-ubiquitination (single ubiquitin) and polyubiquitination (ubiquitin chains) [6]. The ubiquitin-proteasome system (UPS) governs the degradation of over 80% of intracellular proteins, oversees protein quality control, and upholds protein homeostasis [7].…”

Low Protein Expression of Lztr1 in Hepatocellular Carcinoma Triggers Tumorigenesis Via Activating the Ras/Raf/Mek/Erk Signaling

“…Dysregulation of ubiquitination is closely involved in the occurrence and progression of a wide range of tumor types [22], including HCC [23]. Leucine zipper-like transcription regulator 1 (LZTR1), a member of the BTB-Kelch protein family, is a substrate speci c adaptor for the Cullin3-RING E3 ligase (CRL3) ubiquitin ligase complex, regulating a range of cell functions [24].…”