Role of microtubule actin crosslinking factor 1 (MACF1) in bipolar disorder pathophysiology and potential in lithium therapeutic mechanism

Salem, Deepak; Fecek, Ronald J.

doi:10.1038/s41398-023-02483-6

Cited by 5 publications

(1 citation statement)

References 124 publications

(168 reference statements)

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“…This suggests that the SH3 interactions with the PRPs characterized in this study go beyond SOS1 as a binding partner, although the binding specificities of the listed proteins (Figure 4) remain to be investigated. However, several studies confirm the interactions of the identified proteins with SH3DCPs, including zinc finger proteins with p130Cas [28], MACF1 with Spectrin [29], DLGAP with DLG [30], WRCH1/RHOU with GRB2 [31,32], Paxillin with SRC [33,34], and SSTR5 with Homer, Dynamin, IRSp53, and Cortactin [35].…”

Section: Sh3 Domain-prp Relationships Beyond Sos1mentioning

confidence: 93%

Functional Classification and Interaction Selectivity Landscape of the Human SH3 Domain Superfamily

Kazemein Jasemi,

Mehrabipour,

Magdalena Estirado

et al. 2024

Cells

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SRC homology 3 (SH3) domains are critical interaction modules that orchestrate the assembly of protein complexes involved in diverse biological processes. They facilitate transient protein–protein interactions by selectively interacting with proline-rich motifs (PRMs). A database search revealed 298 SH3 domains in 221 human proteins. Multiple sequence alignment of human SH3 domains is useful for phylogenetic analysis and determination of their selectivity towards PRM-containing peptides (PRPs). However, a more precise functional classification of SH3 domains is achieved by constructing a phylogenetic tree only from PRM-binding residues and using existing SH3 domain–PRP structures and biochemical data to determine the specificity within each of the 10 families for particular PRPs. In addition, the C-terminal proline-rich domain of the RAS activator SOS1 covers 13 of the 14 recognized proline-rich consensus sequence motifs, encompassing differential PRP pattern selectivity among all SH3 families. To evaluate the binding capabilities and affinities, we conducted fluorescence dot blot and polarization experiments using 25 representative SH3 domains and various PRPs derived from SOS1. Our analysis has identified 45 interacting pairs, with binding affinities ranging from 0.2 to 125 micromolar, out of 300 tested and potential new SH3 domain-SOS1 interactions. Furthermore, it establishes a framework to bridge the gap between SH3 and PRP interactions and provides predictive insights into the potential interactions of SH3 domains with PRMs based on sequence specifications. This novel framework has the potential to enhance the understanding of protein networks mediated by SH3 domain–PRM interactions and be utilized as a general approach for other domain–peptide interactions.

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Section: Sh3 Domain-prp Relationships Beyond Sos1mentioning

confidence: 93%

Functional Classification and Interaction Selectivity Landscape of the Human SH3 Domain Superfamily

Kazemein Jasemi,

Mehrabipour,

Magdalena Estirado

et al. 2024

Cells

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hnRNP R promotes O-GlcNAcylation of eIF4G and facilitates axonal protein synthesis

Zare,

Salehi,

Bader

et al. 2024

Nat Commun

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Motoneurons critically depend on precise spatial and temporal control of translation for axon growth and the establishment and maintenance of neuromuscular connections. While defects in local translation have been implicated in the pathogenesis of motoneuron disorders, little is known about the mechanisms regulating axonal protein synthesis. Here, we report that motoneurons derived from Hnrnpr knockout mice show reduced axon growth accompanied by lowered synthesis of cytoskeletal and synaptic components in axons. Mutant mice display denervated neuromuscular junctions and impaired motor behavior. In axons, hnRNP R is a component of translation initiation complexes and, through interaction with O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (Ogt), modulates O-GlcNAcylation of eIF4G. Restoring axonal O-GlcNAc levels rescued local protein synthesis and axon growth defects of hnRNP R knockout motoneurons. Together, these findings demonstrate a function of hnRNP R in controlling the local production of key factors required for axon growth and formation of neuromuscular innervations.

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Functional Classification and Interaction Selectivity Landscape of the Human SH3 Domain Superfamily

Jasemi Kazemein,

Mehrabipour,

Magdalena Estirado

et al. 2023

Preprint

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SRC homology 3 (SH3) domains are critical interaction modules that orchestrate the assembly of protein complexes involved in diverse biological processes. They facilitate transient protein-protein interactions by selectively interacting with proline-rich motifs (PRMs). A database search revealed 298 SH3 domains in 221 human proteins. Multiple sequence alignment of human SH3 domains is useful for phylogenetic analysis and determination of their selectivity towards PRM-containing peptides (PRPs). However, a more precise functional classification of SH3 domains is achieved by constructing a phylogenetic tree only from PRM-binding residues and using existing SH3-PRP structures and biochemical data to determine the specificity within each of the 10 families for particular PRPs. In addition, the C-terminal proline-rich domain of the RAS activator SOS1 covers 13 of the 14 recognized proline-rich consensus sequence motifs, encompassing differential PRP pattern selectivity among all SH3 families. To evaluate binding capabilities and affinities, we conducted fluorescence dot blot and polarization experiments using 25 representative SH3 domains and various PRPs derived from SOS1. Our analysis has identified 45 interacting pairs with binding affinities ranging from 0.2 to 125 micromolar out of 300 tested and potential new interactors of SOS1. Furthermore, it establishes a framework to bridge the gap between SH3 and PRP interactions and provides predictive insights into potential interactions of SH3 domains with PRMs based on sequence specifications. This novel framework has the potential to enhance the understanding of protein networks mediated by SH3-PRM interactions and be utilized as a general approach for other domain-peptide interactions.

show abstract

Role of microtubule actin crosslinking factor 1 (MACF1) in bipolar disorder pathophysiology and potential in lithium therapeutic mechanism

Cited by 5 publications

References 124 publications

Functional Classification and Interaction Selectivity Landscape of the Human SH3 Domain Superfamily

Functional Classification and Interaction Selectivity Landscape of the Human SH3 Domain Superfamily

hnRNP R promotes O-GlcNAcylation of eIF4G and facilitates axonal protein synthesis

Functional Classification and Interaction Selectivity Landscape of the Human SH3 Domain Superfamily

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