The Phox homology (PX) domain, a new player in phosphoinositide signalling

Xu, Yongfu; Seet, Li‐Fong; Hanson, Brendon J.; Hong, Wanjin

doi:10.1042/bj3600513

Cited by 93 publications

(37 citation statements)

References 179 publications

(257 reference statements)

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“…SNX27 lacks a recognized BAR domain, is the only known family member containing a PDZ domain, and, except for its PX domain, is largely distinct from other sorting nexins. It is interesting to note that sorting nexin 17 (SNX17), although it lacks a PDZ domain, shares homology with SNX27 elsewhere (Xu et al, 2001) and has been found to promote recycling of the low-density lipoprotein receptor-related protein (LRP) by interacting with a tyrosine-based sequence distinct from a PDZ motif (van Kerkhof et al, 2005). SNX27 could potentially function via PDZ-dependent inhibition of receptor interaction with the lysosomal sorting machinery or, alternatively, by promoting PDZ-directed packaging of receptors into recycling vesicles.…”

Section: Resultsmentioning

confidence: 99%

SNX27 mediates PDZ-directed sorting from endosomes to the plasma membrane

Lauffer

Melero

Temkin

et al. 2010

Journal of Cell Biology

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Section: Resultsmentioning

confidence: 99%

SNX27 mediates PDZ-directed sorting from endosomes to the plasma membrane

Lauffer

Melero

Temkin

et al. 2010

Journal of Cell Biology

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275

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“…Since deletion of these effectors does not lead to all the defects associated with loss of Fab1p, additional effectors remain to be identified. Other proteins that can bind PtdIns(3,5)P 2 (Xu et al, 2001;Cozier et al, 2002) seem unlikely to mediate any of the known effects of this lipid.…”

Section: Introductionmentioning

confidence: 99%

Svp1p defines a family of phosphatidylinositol 3,5-bisphosphate effectors

Dove

Piper

McEwen

et al. 2004

EMBO J

321

495

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Phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2), made by Fab1p, is essential for vesicle recycling from vacuole/lysosomal compartments and for protein sorting into multivesicular bodies. To isolate PtdIns(3,5)P2 effectors, we identified Saccharomyces cerevisiae mutants that display fab1delta-like vacuole enlargement, one of which lacked the SVP1/YFR021w/ATG18 gene. Expressed Svp1p displays PtdIns(3,5)P2 binding of exquisite specificity, GFP-Svp1p localises to the vacuole membrane in a Fab1p-dependent manner, and svp1delta cells fail to recycle a marker protein from the vacuole to the Golgi. Cells lacking Svp1p accumulate abnormally large amounts of PtdIns(3,5)P2. These observations identify Svp1p as a PtdIns(3,5)P2 effector required for PtdIns(3,5)P2-dependent membrane recycling from the vacuole. Other Svp1p-related proteins, including human and Drosophila homologues, bind PtdIns(3,5)P2 similarly. Svp1p and related proteins almost certainly fold as beta-propellers, and the PtdIns(3,5)P2-binding site is on the beta-propeller. It is likely that many of the Svp1p-related proteins that are ubiquitous throughout the eukaryotes are PtdIns(3,5)P2 effectors. Svp1p is not involved in the contributions of FAB1/PtdIns(3,5)P2 to MVB sorting or to vacuole acidification and so additional PtdIns(3,5)P2 effectors must exist.

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“…Nevertheless, these truncated forms would be expected to compete with IRAS-M for membrane anchoring and protein-protein assembly, because the respective PX and leucine-rich repeat domains of IRAS-M are encoded within the first 510 aas. 9,10 Because only transfections with IRAS-M and IRAS-L led to I 1 binding sites in CHO cells (TABLE 3), it seems that the most severely truncated form of IRAS (IRAS-S) lacks the aas necessary to encode an imidazoline binding site. The binding domain for imidazolines has previously been suggested to require acidic aas-specifically those in region #622 through 698 of IRAS-M. 3 IRAS-L also lacks this acidic region but still has imidazoline binding capacity (TABLE 3).…”

Section: Discussionmentioning

confidence: 99%

IRAS Splice Variants

Piletz

Deleersnijder

Roth

et al. 2003

Annals of the New York Academy of Sciences

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The human I(1)-imidazoline receptor candidate gene, iras, has previously been cloned and mapped to locus 3p21.1-9 (also known as Nischarin; accession No. AC006208). By comparison to a database of expressed sequence tags (ESTs), three alternatively spliced transcripts have been deduced. A map of 21 exons was constructed for the medium-length transcript (IRAS-M) containing 5,232 base pairs (bp) and encoding 1,504 amino acids (aas). Introns 13B and 13C are inserted into the two alternative transcripts, forming IRAS-S and IRAS-L mRNA (short and long isoforms). Northern blots confirmed the existence of these mRNA isoforms. In most brain regions the order of mRNA abundance was IRAS-M > IRAS-L > IRAS-S mRNA. Although aas 1 through 510 are theoretically identical, truncated proteins could be derived from IRAS-S (2,678 bp transcript yields 515 aas) and IRAS-L (9,457 bp transcript yields 583 aas). Because exon-16 of the iras gene has been proposed to encode the functional domains of imidazoline and a-5 integrin binding, only IRAS-M is expected to possess I(1) receptor properties. Subtype-selective cDNA expression constructs were therefore generated and used to transfect CHO cells. High-affinity I(1) binding was endowed by IRAS-M and IRAS-L, but not by IRAS-S transfection.

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The Phox homology (PX) domain, a new player in phosphoinositide signalling

Cited by 93 publications

References 179 publications

SNX27 mediates PDZ-directed sorting from endosomes to the plasma membrane

SNX27 mediates PDZ-directed sorting from endosomes to the plasma membrane

Svp1p defines a family of phosphatidylinositol 3,5-bisphosphate effectors

IRAS Splice Variants

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