The EH and SH3 domain Ese proteins regulate endocytosis by linking to dynamin and Eps15

Sengar, Ameet S.; Wang, Wei; Bishay, Joseph; Cohen, Samuel M.; Egan, Sean E.

doi:10.1093/emboj/18.5.1159

Cited by 217 publications

(257 citation statements)

References 51 publications

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“…The Intersectin adaptor protein is thought to function in clathrin-dependent endocytosis by recruiting endocytosis machinery to clathrin-coated pits (Yamabhai et al, 1998;Sengar et al, 1999;Simpson et al, 1999;Koh et al, 2004;Marie et al, 2004). The C. elegans genome contains a single Intersectin orthologue, called ITSN-1, which is most similar to Drosophila dynamin-associated protein of 160 kDa (Dap160) and the short isoform of human ITSN1 ( Figure 5A).…”

Section: Unc-11 and Itsn-1 Function Upstream Of Lin-10 But Not Rab-10mentioning

confidence: 99%

RAB-10 Regulates Glutamate Receptor Recycling in a Cholesterol-dependent Endocytosis Pathway

Glodowski

Chen

Schaefer

et al. 2007

MBoC

104

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Regulated endocytosis of ␣-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid-type glutamate receptors (AMPARs) is critical for synaptic plasticity. However, the specific combination of clathrin-dependent and -independent mechanisms that mediate AMPAR trafficking in vivo have not been fully characterized. Here, we examine the trafficking of the AMPAR subunit GLR-1 in Caenorhabditis elegans. GLR-1 is localized on synaptic membranes, where it regulates reversals of locomotion in a simple behavioral circuit. Animals lacking RAB-10, a small GTPase required for endocytic recycling of intestinal cargo, are similar in phenotype to animals lacking LIN-10, a postsynaptic density 95/disc-large/zona occludensdomain containing protein: GLR-1 accumulates in large accretions and animals display a decreased frequency of reversals. Mutations in unc-11 (AP180) or itsn-1 (Intersectin 1), which reduce clathrin-dependent endocytosis, suppress the lin-10 but not rab-10 mutant phenotype, suggesting that LIN-10 functions after clathrin-mediated endocytosis. By contrast, cholesterol depletion, which impairs lipid raft formation and clathrin-independent endocytosis, suppresses the rab-10 but not the lin-10 phenotype, suggesting that RAB-10 functions after clathrin-independent endocytosis. Animals lacking both genes display additive GLR-1 trafficking defects. We propose that RAB-10 and LIN-10 recycle AMPARs from intracellular endosomal compartments to synapses along distinct pathways, each with distinct sensitivities to cholesterol and the clathrin-mediated endocytosis machinery. INTRODUCTIONContinuous movement of ␣-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA)-type glutamate receptors (AMPARs) into and out of synaptic membranes is a key mechanism for the regulation of excitatory synaptic strength. Previous work has shown that insertion of AMPARs into the plasma membrane strengthens synapses and that it is required to convert silent synapses into active synapses (Bredt and Nicoll, 2003;Malenka, 2003;Malinow, 2003;Sheng and Hyoung Lee, 2003;Gerges et al., 2005). Furthermore, it has recently been shown that recycling of AMPARs from internal endosomal compartments back to the plasma membrane is important for long-term potentiation (Park et al., 2004). By contrast, endocytosis of AMPARs at sites adjacent to the postsynaptic density is important for long-term depression (Carroll et al., 2001;Racz et al., 2004). Thus, molecular machinery required for endocytosis, as well as intracellular membrane trafficking processes, ultimately regulates the character of signal transmitted at each synapse.Multiple endocytosis trafficking pathways have been observed in cells. Clathrin-dependent endocytosis occurs at clathrin-coated pits, where transmembrane protein cargo and adaptor molecules recruit soluble clathrin (Le Roy and Wrana, 2005). Vesicles coated with a clathrin lattice are then pinched off from the membrane. Members of the Rab family of small guanosine triphosphate (GTP)ases mediate the intracellular membrane trafficking of endocytose...

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Section: Unc-11 and Itsn-1 Function Upstream Of Lin-10 But Not Rab-10mentioning

confidence: 99%

RAB-10 Regulates Glutamate Receptor Recycling in a Cholesterol-dependent Endocytosis Pathway

Glodowski

Chen

Schaefer

et al. 2007

MBoC

104

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“…One unique feature of WNK proteins is that they contain multiple PXXP motifs known for binding SH3 domains. A recent study (He et al, 2007) reports that WNK1 and 4 stimulate CCVmediated endocytosis of ROMK by recruiting intersectin, a multimodular endocytic scafford protein containing five SH3 domains (Sengar et al, 1999). The effects of WNK1 and 4 on NCC also occur through changes of membrane expression (Yang et al, 2003;Cai et al, 2006).…”

Section: Mechanisms Of Regulation By Wnksmentioning

confidence: 99%

WNKs: protein kinases with a unique kinase domain

Huang

Kuy²,

Wang³

et al. 2007

Exp Mol Med

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WNKs (with-no-lysine [K]) are a family of serine-threonine protein kinases with an atypical placement of the catalytic lysine relative to all other protein kinases. The roles of WNK kinases in regulating ion transport were first revealed by the findings that mutations of two members cause a genetic hypertension and hyperkalemia syndrome. More recent studies suggest that WNKs are pleiotropic protein kinases with important roles in many cell processes in addition to ion transport. Here, we review roles of WNK kinases in the regulation of ion balance, cell signaling, survival, and proliferation, and embryonic organ development.

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“…Intersectin is a scaffolding protein that has five SH3 domains (SH3A-SH3E), which are sites for protein-protein interactions (Roos and Kelly, 1998;Yamabhai et al, 1998;Sengar et al, 1999). Through its protein interactions, intersectin has been demonstrated to function in endocytosis (Yamabhai et al, 1998;Simpson et al, 1999) and the regulation of actin dynamics , and it has also been implicated in exocytosis (Okamoto et al, 1999).…”

Section: Tuc-4b Interacts With the Sh3a Domain Of Intersectinmentioning

confidence: 99%

TUC-4b, a Novel TUC Family Variant, Regulates Neurite Outgrowth and Associates with Vesicles in the Growth Cone

et al. 2003

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The TUC (TOAD-64/Ulip/CRMP) proteins are homologs of UNC-33, a protein that is required for axon extension and guidance in Caenorhabditis elegans. The TUC proteins are expressed in newly born neurons in the developing nervous system and have been implicated in semaphorin signaling and neuronal polarity. Here, we identify several new variants of the TUC family, each of which is expressed during distinct periods of neural development. We cloned and characterized TUC-4b, a variant of TUC-4a that includes a unique N-terminal extension. The functional relevance of this N-terminal domain is demonstrated by the finding that overexpression of TUC-4b, but not TUC-4a, results in increased neurite length and branching. Furthermore, whereas TUC-4a is expressed throughout life, TUC-4b is expressed exclusively during embryonic development. TUC-4b is localized to SV2 (synaptic vesicle protein 2)-positive vesicles in the central domain of the growth cone, suggesting a potential role in growth cone vesicle transport. Furthermore, TUC-4b interacts with the SH3A (Src homology 3A) domain of intersectin, an endocytic-exocytic adaptor protein. Together, these data suggest that TUC-4b can regulate neurite extension and branching through a mechanism that may involve membrane transport in the growth cone.

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The EH and SH3 domain Ese proteins regulate endocytosis by linking to dynamin and Eps15

Cited by 217 publications

References 51 publications

RAB-10 Regulates Glutamate Receptor Recycling in a Cholesterol-dependent Endocytosis Pathway

RAB-10 Regulates Glutamate Receptor Recycling in a Cholesterol-dependent Endocytosis Pathway

WNKs: protein kinases with a unique kinase domain

TUC-4b, a Novel TUC Family Variant, Regulates Neurite Outgrowth and Associates with Vesicles in the Growth Cone

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