Disease relevance of SNX5

• SNX5, a new member of the sorting nexin family, binds to the Fanconi anemia complementation group A protein [1].

High impact information on SNX5

• Clathrin isoform CHC22, a component of neuromuscular and myotendinous junctions, binds sorting nexin 5 and has increased expression during myogenesis and muscle regeneration [2].
• A loss-of-function screen reveals SNX5 and SNX6 as potential components of the mammalian retromer [3].
• SNX5 forms heterodimers with SNX1 and this interaction is required for endosome association of SNX5 [4].
• Time-lapse videomicroscopy revealed the highly dynamic extension of SNX5-labelled tubules and their departure from the macropinosome body to follow predefined paths towards the perinuclear region of the cell, before fusing with early endosomal acceptor membranes [4].
• Therefore, SNX5 is localized to a subdomain of the early endosome distinct from EEA1 and, following EGF stimulation and elevation of PtdIns3,4P2, is also transiently recruited to the plasma membrane [5].

Biological context of SNX5

• Using this screen, we identified two proteins, SNX5 and SNX6, that, when suppressed, induced a phenotype similar to that observed upon suppression of known retromer components [3].

Anatomical context of SNX5

• Northern blot analysis of SNX5 showed the presence of alternatively spliced transcripts and different expression patterns in various human cancer cell lines and normal tissues [1].
• In response to EGF stimulation, either the SNX5-PX domain or full-length SNX5 was rapidly recruited to the plasma membrane [5].

Associations of SNX5 with chemical compounds

• These results indicate that SNX5 may have functions not only associated with endosomal sorting but also with the phosphoinositide-signalling pathway [5].
• Using liposome-based binding assays, we have shown that the PX domain of SNX5 interacts not only with PtdIns3P but also with PtdIns3,4P2 [5].

Regulatory relationships of SNX5

• Functionally, overexpression of SNX5 inhibits the degradation of EGFR [6].

Other interactions of SNX5

• The intracellular localization of deletion mutants and fusions with green fluorescent protein showed that the C-terminal regions of SNX1 and SNX5 are responsible for their endosomal localization [7].
• We found that overexpression of SNX5 increased FANCA protein levels [1].
• Inhibitory regulation of EGF receptor degradation by sorting nexin 5 [6].

Analytical, diagnostic and therapeutic context of SNX5

• The interaction between FANCA and SNX5 was confirmed by immunoprecipitation studies [1].

References