The N Terminus of Pro-endothelial Monocyte-activating Polypeptide II (EMAP II) Regulates Its Binding with the C Terminus, Arginyl-tRNA Synthetase, and Neurofilament Light Protein

Abstract

Background: Functional domains of pro-EMAP II play an important role in multi-aminoacyl tRNA synthetase (MSC) complexes. Results:The N terminus of Pro-EMAP II binds to its C terminus, arginyl-tRNA synthetase, and the neurofilament light subunit and contains a putative leucine zipper. Conclusion:The N terminus of pro-EMAP II facilitates its interaction with MSC complexes. Significance: Understanding these binding domains may provide important insights into transcriptional regulation.

Aminoacyl tRNA synthetase complex interacting multifunctional protein 1 simultaneously binds Glutamyl-Prolyl-tRNA synthetase and scaffold protein aminoacyl tRNA synthetase complex interacting multifunctional protein 3 of the multi-tRNA synthetase complex

“…2D), although previous studies found that the first 70 a.a. of AIMP1 is sufficient to maintain robust RARS binding (16). These findings suggest that rather the entirety of AIMP1 with an intact intra-molecular N- to C-terminus bond (9) was required for efficient AIMP3 binding. We hypothesize that the interaction site for AIMP3 is formed due to this intramolecular interaction within AIMP1.…”

“…Instead of a GST-L domain found in Arc1p, the AIMP1 N-terminus contains a coiled-coil motif. All previously reported interactions for AIMP1 were mapped to this coiled-coil region (9). In addition, we previously reported intra-molecular bond within the AIMP1 protein (9).…”

“…All previously reported interactions for AIMP1 were mapped to this coiled-coil region (9). In addition, we previously reported intra-molecular bond within the AIMP1 protein (9). Here we report the observation of AIMP1 binding to AIMP3 in addition to independently reported AIMP1 and AIMP2 interaction (15).…”

“…However, AIMP1, the third scaffold protein, has no GST-like domain. Instead, it contains approximately a 70 amino acid (a.a.) long coiled-coil domain, followed by an unstructured region and TRBD domains (9). The AIMP1 coiled-coil domain is further subdivided into two regions; an N terminal part that interacts with the coiled-coil domain of AIMP2 and the distal part that interacts with RARS.…”

Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer

“…Moreover, AIMP1 was a negative regulator of NF phosphorylation, and its overexpression or depletion could change the phosphorylation level of NFs, leading to the NF network disassembly. Recently, Xu et al discovered that the N terminus of AIMP1 was responsible for the binding to its C terminus and arginyl-tRNA synthetase (RARS), and it also colocalized to the NF-L subunit protein 41 . These findings suggest that AIMP1 plays an important role in NF assembly and axon maintenance, which provides a new idea for exploring the pathogenesis of neurological diseases.…”