Hematopoietic lineage cell-specific protein-1 (HS1) binding protein 3 (HS1BP3) associates with HS1 proteins through their SH3 domains, suggesting a role in mediating signaling. It has been reported that HS1BP3 might affect the IL-2 signaling pathway in hematopoietic lineage cells []. Mutations in HS1BP3 may also be associated with familial Parkinson disease and essential tremor [, ]. HS1BP3 contains a PX domain, a leucine zipper, motifs similar to immunoreceptor tyrosine-based inhibitory motif and proline-rich regions [].
Hematopoietic lineage cell-specific protein-1 (HS1) binding protein 3 (HS1BP3) associates with HS1 proteins through their SH3 domains, suggesting a role in mediating signaling. It has been reported that HS1BP3 might affect the IL-2 signaling pathway in hematopoietic lineage cells []. Mutations in HS1BP3 may also be associated with familial Parkinson disease and essential tremor [, ]. HS1BP3 contains a PX domain, a leucine zipper, motifs similar to immunoreceptor tyrosine-based inhibitory motif and proline-rich regions [].This entry represents the PX domain of HS1BP3. In general, the PX domain interacts with PIs and plays a role in targeting proteins to PI-enriched membranes [].
This entry represents a group of DnaJ homologue subfamily C proteins, including GRV2 from Arabidopsis and DNAJC13 (also known as RME-8) from humans. They are involved in endocytosis. GRV2 functions in vesicle trafficking from the multivesicular body/pre-vacuolar compartment to the lytic vacuole []. In Arabidopsis grv2 mutants display enlarged aggregated endosomes, defective vacuole biogenesis and embryogenesis, and reduced gravitropic responses [, , ]. DNAJC13 plays a role in the endosomal transport machinery, in which it coordinates the activity of the WASH complex with the function of the retromer SNX dimer to control endosomal tubulation [].DNAJC13 has been linked to Parkinson disease []. In humans, DNAJC13 localizes to early endosomal compartments via an N-terminal PI(3)P targeting motif and binds the co-chaperone Heat shock cognate-70 (Hsc70) through the central J domain, whereas the remainder interacts with the BAR-domain containing sorting nexin 1 (SNX1) protein and the FAM21 subunit of the WASH complex[].
Formins (formin homology proteins) proteins play a crucial role in the reorganisation of the actin cytoskeleton and associate with the fast-growing end (barbed end) of actin filaments [, ]. This entry represents the formin homologues from plants. Seed plants have two formin clades with numerous paralogues []. They can be classified as class I and class II formins. Class I formins includes a N-terminal membrane insertion signal, a predicted extracytoplasmic Pro-rich stretch, a transmembrane region, and C-terminal FH1 and FH2 domains []. Though class II formins usually contain a N-terminal PTEN domain related to the human PTEN protein (implied in pathogenesis of the Parkinson disease) [], the N-termini of type-II plant formins do not contain any recognisable domain that can provide a clue to their biological function.
This entry represents eukaryotic translation initiation factor 4 gamma 1 (EIF4G1), which is a component of the eIF4F complex. The eIF4F complex is required for recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome. Mitogen-activated protein kinases control translation by post-translational modification of translation initiation factors, and eIF4G1 is a substrate for protein kinase C []. As part of the eIF4F complex, EIF4G1 mediates endoplasmic reticulum stress-induced ATF4 (a master stress-induced transcription factor) mRNA translation []. Mutations in the EIF4G1 gene cause Parkinson disease 18, which is a neurodegenerative disorder with the following symptoms: bradykinesia, resting tremor, muscular rigidity and postural instability, and loss of dopaminergic neurons from the substantia nigra []. Viral infection can lead to the shutdown of translation by cleavage of EIF4G1, for example, by HIV-1 retropepsin [], rhinovirus picornain 2A []and foot-and-mouth disease virus L-peptidase [].
This is the N-terminal domain of DNAJC13/GVR2, which is required for membrane association and interaction with FAM21 tail domain []. It contains critical residues mediating phosphatidylinositol 3-phosphate (PI(3)P) binding, required for its association with endosomes [].This entry represents a group of DnaJ homologue subfamily C proteins, including GRV2 from Arabidopsis and DNAJC13 (also known as RME-8) from humans. They are involved in endocytosis. GRV2 functions in vesicle trafficking from the multivesicular body/pre-vacuolar compartment to the lytic vacuole []. In Arabidopsis grv2 mutants display enlarged aggregated endosomes, defective vacuole biogenesis and embryogenesis, and reduced gravitropic responses [, , ]. DNAJC13 plays a role in the endosomal transport machinery, in which it coordinates the activity of the WASH complex with the function of the retromer SNX dimer to control endosomal tubulation [].DNAJC13 has been linked to Parkinson disease []. In humans, DNAJC13 localizes to early endosomal compartments via an N-terminal PI(3)P targeting motif and binds the co-chaperone Heat shock cognate-70 (Hsc70) through the central J domain, whereas the remainder interacts with the BAR-domain containing sorting nexin 1 (SNX1) protein and the FAM21 subunit of the WASH complex[].
