Semaphorin3a Enhances Endocytosis at Sites of Receptor–F-Actin Colocalization during Growth Cone Collapse

Fournier, Alyson E.; Nakamura, Fumio; Kawamoto, Susumu; Goshima, Yoshio; Kalb, Robert G.; Strittmatter, Stephen M.

doi:10.1083/jcb.149.2.411

Cited by 197 publications

(185 citation statements)

References 48 publications

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“…Stimulation of growth cones by semaphorins or ephrins induces endocytosis in the growth cone (Fournier et al, 2000;Jurney et al, 2002). However, endocytosis is not stimulated by cytochalasin B, suggesting that endocytosis is not a nonspecific consequence of collapse but rather the specific result of intracellular signaling in response to guidance cues.…”

Section: Tuc-4b May Regulate Vesicle Function In the Growth Conementioning

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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Section: Tuc-4b May Regulate Vesicle Function In the Growth Conementioning

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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“…Therefore, SEMA4B might function as a CLCP1 receptor. Sema3A-neuropilin interactions induce neuropilin-1 endocytosis, which is mediated by L1-CAM (Fournier et al, 2000;Castellani et al, 2004), which in turn modulates growth cone sensitivity to semaphorin repulsion signals. CLCP1 degradation after CLCP1-SEMA4B interaction may indicate an induction of CLCP1 endocytosis by SEMA4B.…”

Section: Clcp1 Regulates Lung Cancer Cell Motility With Sema4bmentioning

confidence: 99%

CLCP1 interacts with semaphorin 4B and regulates motility of lung cancer cells

et al. 2007

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We previously established a highly metastatic subline, LNM35, from the NCI-H460 lung cancer cell line, and demonstrated upregulation of a novel gene, CLCP1 (CUB, LCCL-homology, coagulation factor V/VIII homology domains protein), in LNM35 and lung cancer specimens. In this study, we focused on the potential roles of that gene in cancer metastasis. First, we established stable LNM35 RNAi clones, in which CLCP1 expression was suppressed by RNAi, and found that their motility was significantly reduced, although growth rates were not changed. Next, in vitro selection of a phage display library demonstrated that a phage clone displaying a peptide similar to a sequence within the Sema domain of semaphorin 4B (SEMA4B) interacted with LNM35. Immunoprecipitation experiments confirmed interaction of CLCP1 with SEMA4B, regulation of CLCP1 protein by ubiquitination and proteasome degradation enhanced in the presence of SEMA4B. These results are the first to indicate that CLCP1 plays a role in cell motility, whereas they also showed that at least one of its ligands is SEMA4B and that their interaction mediates proteasome degradation by CLCP1. Although the physiological role of the interaction between CLCP1 and SEMA4B remains to be investigated, this novel gene may become a target of therapy to inhibit metastasis of lung cancers.

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“…Dissociated E13 chick dorsal root ganglia (DRG) neurons were grown for 4 -8 hr, fixed, and stained with phalloidin, and neurite outgrowth lengths were assessed using N IH Image. GSTNogo-66 and myelin were prepared as described previously (Fournier et al, 2000b;GrandPre et al, 2000). Aggrecan was obtained from Sigma (St. L ouis, MO).…”

Section: Methodsmentioning

confidence: 99%

Truncated Soluble Nogo Receptor Binds Nogo-66 and Blocks Inhibition of Axon Growth by Myelin

et al. 2002

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Semaphorin3a Enhances Endocytosis at Sites of Receptor–F-Actin Colocalization during Growth Cone Collapse

Cited by 197 publications

References 48 publications

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

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

CLCP1 interacts with semaphorin 4B and regulates motility of lung cancer cells

Truncated Soluble Nogo Receptor Binds Nogo-66 and Blocks Inhibition of Axon Growth by Myelin

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