Interaction of the Rho Family Small G Proteins with Kinectin, an Anchoring Protein of Kinesin Motor

Hotta, Kenji; Tanaka, Kazuma; Mino, Akihisa; Kohno, H.; Takai, Yoshimi

doi:10.1006/bbrc.1996.1132

Cited by 65 publications

(41 citation statements)

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“…It is possible that kinesin is responsible for delivering F-actin regulating proteins to the phagocytic cup. The Rho family of small GTPases involved in actin polymerization and cell motility, including rhoA, rac1, and cdc42, has been associated with kinectin, a vesicle membrane protein that binds to kinesin (40,41). Equally plausible is that reduced delivery of FcRs to the surface results in sparser receptor ligation and downstream signaling that causes attenuated actin cup formation.…”

Section: Discussionmentioning

confidence: 99%

Kinesin 5B Is Necessary for Delivery of Membrane and Receptors during FcγR-Mediated Phagocytosis

Silver

Harrison

2011

The Journal of Immunology

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FcγR-mediated phagocytosis is a cellular event that is evolutionary conserved to digest IgG-opsonized pathogens. Pseudopod formation during phagocytosis is a limiting step in managing the uptake of particles, and in this paper, we show that the conventional kinesin is involved in both receptor and membrane delivery to the phagocytic cup. Expression of a mutant kinesin isoform (GFP dominant negative mutant of kinesin H chain [EGFP-Kif5B-DN]) in RAW264.7 cells significantly reduced binding of IgG–sheep RBCs when macrophages were faced with multiple encounters with opsonized particles. Scanning electron microscopy analysis of EGFP-Kif5B-DN–expressing cells challenged with two rounds of IgG–sheep RBCs showed sparse, extremely thin pseudopods. We saw disrupted Rab11 trafficking to the phagocytic cup in EGFP-Kif5B-DN–transfected cells. Our particle overload assays also implicated phagosome membrane recycling in pseudopod formation. We observed reduced phagosome fission and trafficking in mutant kinesin-expressing cells, as well as reduced cell surface expression of FcγRs and Mac-1 receptors. In conclusion, anterograde trafficking via kinesin is essential for both receptor recycling from the phagosome and delivery of Rab11-containing membrane stores to effect broad and functional pseudopods during FcγR-mediated phagocytosis.

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Section: Discussionmentioning

confidence: 99%

Kinesin 5B Is Necessary for Delivery of Membrane and Receptors during FcγR-Mediated Phagocytosis

Silver

Harrison

2011

The Journal of Immunology

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“…Kinetic analysis based on the sensorgram yielded the apparent dissociation constant of 34 nM. No significant binding was observed for His 6 to the GST-bait D. …”

Section: The Translation Elongation Factor-1 Delta Interacts Withmentioning

confidence: 97%

“…The kinesin-binding domain can interact with the cargo-binding site of the conventional kinesin and enhance the kinesin's microtubule-stimulated ATPase activity (5). A separate domain interacts with small G-proteins such as Rho A and Rac 1 (6,7) and plays a key role in mediating the microtubule-dependent Rho G activity (8). The role of kinectin in organelle motility is further supported by antibody inhibition and kinectin-domain overexpression studies, in which the organelle motility is adversely affected both in vitro and in vivo (2,5).…”

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confidence: 99%

Kinectin Anchors the Translation Elongation Factor-1δ to the Endoplasmic Reticulum

Ong

et al. 2003

Journal of Biological Chemistry

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Kinectin has been proposed to be a membrane anchor for kinesin on intracellular organelles. A kinectin isoform that lacks a major portion of the kinesin-binding domain does not bind kinesin but interacts with another resident of the endoplasmic reticulum, the translation elongation factor-1 delta (EF-1␦). This was shown by yeast two-hybrid analysis and a number of in vitro and in vivo assays. EF-1␦ provides the guanine nucleotide exchange activities on EF-1␣ during elongation step of protein synthesis. The minimal EF-1␦-binding domain on kinectin resides within a conserved region present in all the kinectin isoforms. Overexpression of the kinectin fragments in vivo disrupted the intracellular localization of EF-1␦ proteins. This report provides evidence of an alternative kinectin function as the membrane anchor for EF-1␦ on the endoplasmic reticulum and provides clues to the EF-1 complex assembly and anchorage on the endoplasmic reticulum.

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“…These include ROCK I (20), ROCK II (21), PRK I (22), PRK II (23), p140mDia (24), rhotekin (25), rhophilin (22), citron kinase (CRIK) (26), kinectin (27), p116RIP (28), and the myosin binding subunit of myosin phosphatase (29). However, the evidence linking particular RhoA effector proteins to the transformation phenotype is still somewhat limited.…”

mentioning

confidence: 99%

Transformation by the Rho-specific Guanine Nucleotide Exchange Factor Dbs Requires ROCK I-mediated Phosphorylation of Myosin Light Chain

Liu

Костенко²,

Mahon

et al. 2006

Journal of Biological Chemistry

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Dbs was identified in a cDNA-based expression screen for sequences that can cause malignant growth when expressed in murine fibroblasts. In previous studies we have shown that Dbs is a Rho-specific guanine nucleotide exchange factor that can activate RhoA and/or Cdc42 in a cell-specific manner. In this current study we have used a combination of genetic and pharmacological approaches to examine the relative contributions of RhoA⅐PRK and RhoA⅐ROCK signaling to Dbs transformation. Our analysis indicates that ROCK is activated in Dbs-transformed cells and that Dbs transformation is dependent upon ROCK I activity. In contrast, there appears to be no requirement for PRK activation in Dbs transformation. Dbs transformation is also associated with increased phosphorylation of myosin light chain and stress fiber formation, both of which occur in a ROCK-dependent manner. Suppression of myosin light chain expression by small interfering RNAs impairs Dbs focus formation, thus establishing a direct link between actinomyosin contraction and Rho-specific guanine nucleotide exchange factor transformation.

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Interaction of the Rho Family Small G Proteins with Kinectin, an Anchoring Protein of Kinesin Motor

Cited by 65 publications

References 0 publications

Kinesin 5B Is Necessary for Delivery of Membrane and Receptors during FcγR-Mediated Phagocytosis

Kinesin 5B Is Necessary for Delivery of Membrane and Receptors during FcγR-Mediated Phagocytosis

Kinectin Anchors the Translation Elongation Factor-1δ to the Endoplasmic Reticulum

Transformation by the Rho-specific Guanine Nucleotide Exchange Factor Dbs Requires ROCK I-mediated Phosphorylation of Myosin Light Chain

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