Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes

Cheever, Matthew L.; Sato, Trey K.; Beer, Tonny de; Kutateladze, Tatiana G.; Emr, Scott D.; Overduin, Michael

doi:10.1038/35083000

Cited by 354 publications

(347 citation statements)

References 39 publications

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“…These findings are in agreement with those observed in other C2 domains, which typically exhibit highly variable and relatively low lipid specificity [18]. Phospholipid binding by the C2 domain was at most ∼60 % of the total protein when compared with the Vam7p PX domain ( Figure 1B), a PtdIns3P binding domain [29]. These results indicate that the Tollip C2 domain preferentially binds phosphatidylinositol species with phosphate groups at their inositol rings.…”

Section: The Tollip C2 Domain Preferentially Binds Phosphoinositidessupporting

confidence: 81%

“…Moreover, Zhang and colleagues have further investigated this phenomenon, and they have found that the down-regulation of transcriptional level of R proteins helps plants to prevent autoimmunity (29).…”

Section: Plant Defense Mechanism: Looks Simple But Actually Notmentioning

confidence: 99%

“…The Vam7p PX domain binds PtdIns3P [29] and was employed as a positive control. In all cases, proteins exhibited fast association and dissociation rates.…”

Section: Kinetic Analysis Of Tollip C2 Domain-phosphoinositide Interamentioning

confidence: 99%

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Structural Basis for Interactions of thePhytophthora sojaeRxLR Effector Avh5 with Phosphatidylinositol 3-Phosphate and for Host Cell Entry

Sun¹,

Kale²,

Azurmendi³

et al. 2013

MPMI

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Oomycetes, such as Phytophthora sojae, are plant pathogens that employ protein effectors that enter host cells to facilitate infection. Plants may overcome infection by recognizing pathogen effectors via intracellular receptors (R proteins) that form part of their defense system. Entry of some effector proteins into plant cells is mediated by conserved RxLR motifs in the effectors and phosphoinositides (PIPs) resident in the host plasma membrane such as phosphatidylinositol 3-phosphate (PtdIns(3)P). Recent reports differ regarding the regions on RxLR effector proteins involved in PIP recognition. To clarify these differences, I have structurally and functionally characterized the P. sojae effector, avirulence homolog-5 (Avh5).

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Section: The Tollip C2 Domain Preferentially Binds Phosphoinositidessupporting

confidence: 81%

Section: Plant Defense Mechanism: Looks Simple But Actually Notmentioning

confidence: 99%

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Structural Basis for Interactions of thePhytophthora sojaeRxLR Effector Avh5 with Phosphatidylinositol 3-Phosphate and for Host Cell Entry

Sun¹,

Kale²,

Azurmendi³

et al. 2013

MPMI

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“…© 2005 by The American Society for Cell Biology nexin (SNX) family of structurally and functionally diverse proteins, defined by the presence of a phox (phagocyte oxidase) homology domain (PX) that encodes a proline-rich sequence and an upstream phospholipid-binding domain (Cheever et al, 2001). So far, 25 human SNXs have been identified and recent studies have uncovered a role for several of these proteins in membrane trafficking (Worby and Dixon, 2002).…”

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confidence: 99%

SNX9 Regulates Dynamin Assembly and Is Required for Efficient Clathrin-mediated Endocytosis

Soulet

Yarar

Leonard

et al. 2005

MBoC

181

233

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Dynamin, a central player in clathrin-mediated endocytosis, interacts with several functionally diverse SH3 domaincontaining proteins. However, the role of these interactions with regard to dynamin function is poorly defined. We have investigated a recently identified protein partner of dynamin, SNX9, sorting nexin 9. SNX9 binds directly to both dynamin-1 and dynamin-2. Moreover by stimulating dynamin assembly, SNX9 stimulates dynamin's basal GTPase activity and potentiates assembly-stimulated GTPase activity on liposomes. In fixed cells, we observe that SNX9 partially localizes to clathrin-coated pits. Using total internal reflection fluorescence microscopy in living cells, we detect a transient burst of EGFP-SNX9 recruitment to clathrin-coated pits that occurs during the late stages of vesicle formation and coincides spatially and temporally with a burst of dynamin-mRFP fluorescence. Transferrin internalization is inhibited in HeLa cells after siRNA-mediated knockdown of SNX9. Thus, our results establish that SNX9 is required for efficient clathrin-mediated endocytosis and suggest that it functions to regulate dynamin activity. INTRODUCTIONThe GTPase dynamin plays a critical role in clathrin-mediated endocytosis (CME; Hinshaw, 2000). Dynamin self-assembles into a collar-like structure around the necks of deeply invaginated clathrin-coated pits (CCPs) where it is believed to directly mediate membrane fission and vesicle release. Dynamin is also associated with newly formed coated pits (Damke et al., 1994;Evergren et al., 2004) where it may function to regulate early stages of coated pit maturation (Sever et al., 2000a;Song and Schmid, 2003;Song et al., 2004).Although only one isoform of dynamin exists in Drosophila and in Caenorhabditis elegans, mammals express at least three isoforms, which are ϳ70% identical to each other. Dynamin-1, the first identified protein in the dynamin family, is expressed exclusively in neuronal cells where it functions in synaptic vesicle recycling (Shpetner and Vallee, 1989;Nakata et al., 1991;Sontag et al., 1994). Dynamin-2 is ubiquitously expressed (Cook et al., 1994;Sontag et al., 1994) and localizes to endocytic CCPs where it functions, like dynamin-1, in endocytosis (Damke et al., 1994;Altschuler et al., 1998). However, dynamin-2 may also be involved in vesicle formation at the Golgi Kreitzer et al., 2000), in regulating actin dynamics (Schafer, 2004), in cell signaling (Kranenburg et al., 1999;Fish et al., 2000), and has recently been localized to the centriole (Thompson et al., 2004). Dynamin-3, which is most highly expressed in testis but also detectable in neurons (Gray et al., 2003) and in lung (Nakata et al., 1993), has been less well studied.Dynamins are atypical GTPases, distinguished by their large size, low affinity for GTP, and high intrinsic rates of GTP hydrolysis (Sever et al., 2000b;Song and Schmid, 2003). Moreover, dynamin can self-assemble in solution (Hinshaw and Schmid, 1995) or on liposome templates into rings and spiral-like structures (Stowell et al., 199...

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“…So far, PX domains are found in over 100 known and hypothetical eukaryotic proteins. The physiological function of the PX domain was only revealed recently by several independent studies (Cheever et al, 2001;Ellson et al, 2001;Kanai et al, 2001;Song et al, 2001;Xu et al, 2001a,b). The majority of PX domains shows binding to phosphatidylinositol 3-monophosphate (PtdIns(3)P), an association that allows the host protein to localize to membranes of the endocytic pathway (Cozier et al, 2002).…”

Section: Discussionmentioning

confidence: 99%

cDNA cloning and characterization of a novel SNX gene differentially expressed in previtellogenic oocytes of gibel carp

Wen

Xie

Gui

2003

Comparative Biochemistry and Physiology Part B: Biochemistry an

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Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes

Cited by 354 publications

References 39 publications

Structural Basis for Interactions of thePhytophthora sojaeRxLR Effector Avh5 with Phosphatidylinositol 3-Phosphate and for Host Cell Entry

Structural Basis for Interactions of thePhytophthora sojaeRxLR Effector Avh5 with Phosphatidylinositol 3-Phosphate and for Host Cell Entry

SNX9 Regulates Dynamin Assembly and Is Required for Efficient Clathrin-mediated Endocytosis

cDNA cloning and characterization of a novel SNX gene differentially expressed in previtellogenic oocytes of gibel carp

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