Characterization of KIF1C, a New Kinesin-like Protein Involved in Vesicle Transport from the Golgi Apparatus to the Endoplasmic Reticulum

Dorner, Cornelia; Ciossek, Thomas; Müller, Susanne; Møller, Niels; Ullrich, Axel; Lammers, Reiner

doi:10.1074/jbc.273.32.20267

Cited by 125 publications

(121 citation statements)

References 60 publications

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“…Further investigation for other isoforms of KIF1B may help us to understand the function of KIF1B. Kif1C is localized primarily at the Golgi apparatus, and is thought to be involved in transporting Golgi membrane (Dorner et al, 1998). The Kif1C can also form dimers and is associated with proteins of the 14-3-3 family (Dorner et al, 1999).…”

Section: Discussionmentioning

confidence: 99%

Genomic structure and mutational analysis of the human KIF1B gene which is homozygously deleted in neuroblastoma at chromosome 1p36.2

et al. 2001

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In order to clone candidate tumor suppressor genes whose loss contributes to the pathogenesis of neuroblastoma (NB), we performed polymerase chain reaction (PCR) screening using a high-density sequence tagged site-content map within a commonly deleted region (chromosome band 1p36) in 24 NB cell lines. We found a *480 kb homozygously deleted region at chromosome band 1p36.2 in one of the 24 NB cell lines, NB-1, and cloned the human homologue (KIF1B-b) of the mouseKif1B-b gene in this region. The KIF1B-b gene had at least 47 exons, all of which had a classic exon ± intron boundary structure. Mouse Kif1B is a microtubule-based putative anterograde motor protein for the transport of mitochondria in neural cells. We performed mutational analysis of the KIF1B-b gene in 23 cell lines using 46 sets of primers and also an allelic imbalance (AI) analysis of KIF1B-b in 50 fresh NB samples. A missense mutation at codon 1554, GTG (Gly) to ATG (Met), silent mutations at codon 409 (ACG to ACA) and codon 1721 (ACC to ACT), and polymorphisms at codon 170, GAT (Asp) to GAA (Glu), and at codon 1087, TAT (Tyr), to TGT (Cys), were all identi®ed, although their functional signi®cances remain to be determined. The AI for KIF1B-b was slightly higher (38%) than those for the other two markers (D1S244, D1S1350) (35 and 32%) within the commonly deleted region (1p36). Reverse transcriptase-PCR analysis of the KIF1B-b gene revealed obvious expression in all NB cell lines except NB-1, although decreased expression of the KIF1B-b gene was found in a subset of early-and advanced-stage NBs. These results suggest that the KIF1B-b gene may not be a candidate for tumor suppressor gene of NB. Oncogene (2001) 20, 5075 ± 5083.

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Section: Discussionmentioning

confidence: 99%

Genomic structure and mutational analysis of the human KIF1B gene which is homozygously deleted in neuroblastoma at chromosome 1p36.2

et al. 2001

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“…Watters et al (17) identified a mutation on a gene named kif1C that is responsible for the different sensitivities of macrophages to LeTx. kif1C encodes a kinesin-like motor protein of the UNC104 subfamily (18). It is clear that proper function of kif1C is required for LeTx resistance, but how this protein is involved in LeTx-elicited changes in macrophages is unknown (17).…”

Section: Anthrax Infections Are Initiated By Endospores Ofmentioning

confidence: 99%

Sensitizing Anthrax Lethal Toxin-resistant Macrophages to Lethal Toxin-induced Killing by Tumor Necrosis Factor-α

Kim

Jing

Hoebe

et al. 2003

Journal of Biological Chemistry

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Macrophages from different inbred mouse strains exhibit striking differences in their sensitivity to anthrax lethal toxin (LeTx)-induced cytolysis. Although LeTxinduced cytolysis of macrophages plays an important role in the outcome of anthrax infection, the sensitivity of macrophages in vitro does not correlate with in vivo susceptibility to infection of Bacillus anthracis. This divergence suggests that additional factors other than LeTx are involved in the cytolysis of LeTx-resistant macrophages in vivo. We found that LeTx-resistant macrophages became sensitive to LeTx-induced cytolysis when these cells were activated by bacterial components. Tumor necrosis factor-␣ induced by bacterial components was a key factor that cooperated with LeTx in inducing LeTx-resistant macrophage death. Tumor necrosis factor-␣/LeTx-induced death of LeTx-resistant macrophages was dependent on mTor (mammalian target of rapamycin), but independent of caspases. Our data indicate that host responses to anthrax infection contribute to cytolysis of LeTx-resistant macrophages.

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“…An intervening sequence of about 580 residues without apparent homology to known proteins separates the FERM and the PTP domains. PTPD1 regulates signaling induced by Tec family members of membrane receptors (19) and associates with KIF1C, a tyrosine-phosphorylated kinesin-like protein that controls retrograde transport of vesicles from the Golgi apparatus to the endoplasmic reticulum (20). Expression of PTPD1 is significantly elevated in several human cancers (21).…”

mentioning

confidence: 99%

Protein-tyrosine Phosphatase PTPD1 Regulates Focal Adhesion Kinase Autophosphorylation and Cell Migration

Carlucci

Gedressi

Lignitto

et al. 2008

Journal of Biological Chemistry

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PTPD1 is a cytosolic nonreceptor tyrosine phosphatase and a positive regulator of the Src-epidermal growth factor transduction pathway. We show that PTPD1 localizes along actin filaments and at adhesion plaques. PTPD1 forms a stable complex via distinct molecular modules with actin, Src tyrosine kinase, and focal adhesion kinase (FAK), a scaffold protein kinase enriched at adhesion plaques. Overexpression of PTPD1 promoted cell scattering and migration, short hairpin RNA-mediated silencing of endogenous PTPD1, or expression of PTPD1 mutants lacking either catalytic activity (PTPD1 C1108S ) or the FERM domain (PTPD1 ⌬1-325 ) significantly reduced cell motility. PTPD1 and Src catalytic activities were both required for epidermal growth factor-induced FAK autophosphorylation at its active site and for downstream propagation of ERK1/2 signaling. Our findings demonstrate that PTPD1 is a component of a multivalent scaffold complex nucleated by FAK at specific intracellular sites. By modulating Src-FAK signaling at adhesion sites, PTPD1 promotes the cytoskeleton events that induce cell adhesion and migration.

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Characterization of KIF1C, a New Kinesin-like Protein Involved in Vesicle Transport from the Golgi Apparatus to the Endoplasmic Reticulum

Cited by 125 publications

References 60 publications

Genomic structure and mutational analysis of the human KIF1B gene which is homozygously deleted in neuroblastoma at chromosome 1p36.2

Genomic structure and mutational analysis of the human KIF1B gene which is homozygously deleted in neuroblastoma at chromosome 1p36.2

Sensitizing Anthrax Lethal Toxin-resistant Macrophages to Lethal Toxin-induced Killing by Tumor Necrosis Factor-α

Protein-tyrosine Phosphatase PTPD1 Regulates Focal Adhesion Kinase Autophosphorylation and Cell Migration

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