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The C-terminal tail of UNC-60B (actin depolymerizing factor/cofilin) is critical for maintaining its stable association with F-actin and is implicated in the second actin-binding site

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JOURNAL OF BIOLOGICAL CHEMISTRY 2001年第8期276卷 5952-5958页

作者： Ono, S McGough, A Pope, BJ Tolbert, VT Bui, A Pohl, J Benian, GM Gernert, KM Weeds, AG Emory Univ Dept Pathol Atlanta GA 30322 USA MRC Mol Biol Lab Cambridge CB2 2QH England Purdue Univ Dept Sci Biol W Lafayette IN 47907 USA Emory Univ Winship Canc Inst Microchem Facil Atlanta GA 30322 USA Frederick Douglas High Sch Decatur GA 30030 USA Emory Univ BIMCORE Atlanta GA 30322 USA

Actin depolymerizing factor (ADF)/cofilin changes the twist of actin filaments by binding two longitudinally associated actin subunits, In the absence of an atomic model of the ADF/cofilin-F-actin complex, we have identified residues in ADF/cofilin that are essential for filament binding. Here, we have characterized the C-terminal tail of UNC-60B (a nematode ADF/cofilin isoform) as a novel determinant for its association with F-actin, Removal of the C-terminal isoleucine (Ile(152)) by carboxypeptidase A or truncation by mutagenesis eliminated F-actin binding activity but strongly enhanced actin depolymerizing activity, Replacement of Ile(152) by Ala had a similar but less marked effect;F-actin binding was weakened and depolymerizing activity slightly enhanced. Truncation of both Arg(151) and Ile(152) or replacement of Arg(151) with Ala also abolished F-actin binding and enhanced depolymerizing activity. Loss of F-actin binding in these mutants was accompanied by loss or greatly decreased severing activity. All of the variants of UNC-60B interacted with G-actin in an indistinguishable manner from wild type. Cryoelectron microscopy showed that UNC-60B changed the twist of F-actin to a similar extent to vertebrate ADF/cofilins. Helical reconstruction and structural modeling of UNC-60B-F-actin complex reveal how the C terminus of UNC-60B might be involved in one of the two actin-binding sites.

关键词：肌动蛋白解聚因子类肌动蛋白类/化学肌动蛋白类/代谢氨基酸序列结合部位漂亮新小杆线虫蛋白质类破解蛋白质蠕虫蛋白质类/化学蠕虫蛋白质类/遗传学蠕虫蛋白质类/代谢异亮氨酸微丝蛋白质类/化学微丝蛋白质类/遗传学微丝蛋白质类/代谢模型分子分子序列数据蛋白质结合序列同源性氨基酸

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Olfactory receptor trafficking involves conserved regulatory steps

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JOURNAL OF BIOLOGICAL CHEMISTRY 2001年第10期276卷 7285-7290页

作者： Gimelbrant, AA Haley, SL McClintock, TS Univ Kentucky Med Ctr Dept Physiol Lexington KY 40536 USA

Olfactory receptors are difficult to functionally express in heterologous cells. They are typically retained in the endoplasmic reticulum of cells commonly used for functional expression studies and are only released to the plasma membrane in mature cells of the olfactory receptor neuron lineage. A recently developed olfactory cell line, odora, traffics olfactory receptors to the plasma membrane when differentiated. We found that undifferentiated odora cells do not traffic olfactory receptors to their surface, even though they release the receptors to the Golgi apparatus and endosomes. This behavior differs from other cell lines tested thus far. Differentiated odora cells also properly traffic vomeronasal receptors of the VN1 type, which lack sequence similarity to olfactory receptors. ODR-4, a protein that is necessary for plasma membrane trafficking of a chemosensory receptor in nematodes, facilitates trafficking of rat olfactory receptor U131 in odora and Chinese hamster ovary cells. Olfactory receptor trafficking from the endoplasmic reticulum to the plasma membrane involves at least two steps whose regulation depends on the maturation state of cells in the olfactory receptor neuron lineage. These results also indicate that some components of the regulatory mechanism are conserved.

关键词： CHO细胞漂亮新小杆线虫蛋白质类细胞分化细胞系细胞膜/代谢仓鼠亚科内质网/代谢内颗粒/代谢高尔基体/代谢免疫组织化学显微镜检查共焦模型生物学嗅觉受体神经元/代谢蛋白质转运受体有气味性物质/代谢受体有气味性物质/生理学重组蛋白质类/代谢转染动物大鼠

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Molecular cloning and characterization of DEFCAP-L and -S, two isoforms of a novel member of the mammalian Ced-4 family of apoptosis proteins

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JOURNAL OF BIOLOGICAL CHEMISTRY 2001年第12期276卷 9230-9238页

作者： Hlaing, T Guo, RF Dilley, KA Loussia, JM Morrish, TA Shi, MM Vincenz, C Ward, PA Univ Michigan Sch Med Dept Pathol Ann Arbor MI 48109 USA Univ Michigan Sch Med Dept Human Genet Ann Arbor MI 48109 USA Pfizer Global Res & Dev Drug Safety Evaluat Ann Arbor MI 48105 USA

We report the deduced amino acid sequences of two alternately spliced isoforms, designated DEFCAP-L and -S, that differ in 44 amino acids and encode a novel member of the mammalian Ced-4 family of apoptosis proteins. Similar to the other mammalian Ced-4 proteins (Apaf-1 and Nod1), DEFCAP contains a caspase recruitment domain (CARD) and a putative nucleotide binding domain, signified by a consensus Walker's A box (P-loop) and B box (Mg2+-binding site). Like Nod1, but different from Apaf-1, DEFCAP contains a putative regulatory domain containing multiple leucine-rich repeats (I;RR). However, a distinguishing feature of the primary sequence of DEFCAP is that DEFCAP contains at its NH,terminus a pyrin-like motif and a proline-rich sequence, possibly involved in protein-protein interactions with Src homology domain 3-containing proteins. By using in vitro coimmunoprecipitation experiments, both long and short isoforms were capable of strongly interacting with caspase-2 and exhibited a weaker interaction with caspase-9, Transient overexpression of full-length DEFCAP-L, but not DEFCAP-S, in breast adenocarcinoma cells MCF7 resulted in significant levels of apoptosis, lie. vitro death assays with transient overexpression of deletion constructs of both isoforms using P-galactosidase as a reporter gene in MCF7 cells suggest the following: 1) the nucleotide binding domain may act as a negative regulator of the killing activity of DEFCAP;2) the LRR/CARD represents a putative constitutively active inducer of apoptosis;3) the killing activity of LRR/CARD is inhibitable by benzyloxycarbonyl-Val-Ala-Asp (OMe)-fluoromethyl ketone and to a lesser extent by Asp-Glu-Val-Asp (OMe)-fluoromethyl ketone;and 4) the CARD is critical for killing activity of DEFCAP;These results suggest that DEFCAP is a novel member of the mammalian Ced-4 family of proteins capable of inducing apoptosis, and understanding its regulation may elucidate the complex nature of the mammalian apoptosis-promoting mach

关键词：衔接蛋白质类信号转导氨基酸序列细胞凋亡凋亡调节蛋白质类碱基序列漂亮新小杆线虫蛋白质类钙结合蛋白质类/化学钙结合蛋白质类/遗传学载体蛋白质类/化学载体蛋白质类/遗传学细胞系染色体图克隆分子 DNA 互补蠕虫蛋白质类/化学蠕虫蛋白质类/遗传学分子序列数据诱变定点蛋白质亚型/遗传学 RNA 信使/遗传学重组融合蛋白质类/代谢序列同源性氨基酸人类

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The survivin-like C-elegans BIR-1 protein acts with the aurora-like kinase AIR-2 to affect chromosomes and the spindle midzone

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MOLECULAR CELL 2000年第2期6卷 211-223页

作者： Speliotes, EK Uren, A Vaux, D Horvitz, HR MIT Howard Hughes Med Inst Dept Biol Cambridge MA 02139 USA PO Royal Melbourne Hosp Walter & Eliza Hall Inst Med Res Melbourne Vic 3050 Australia

Baculoviral IAP repeat proteins (BIRPs) may affect cell death, cell division, and tumorigenesis. The C. elegans BIRP BIR-l was localized to chromosomes and to the spindle midzone. Embryos and fertilized oocytes lacking BIR-1 had defects in chromosome behavior, spindle midzone formation, and cytokinesis. We observed indistinguishable defects in fertilized oocytes and embryos lacking the Aurora-like kinase AIR-2. AIR-2 was not present on chromosomes in the absence of BIR-I. Histone H3 phosphorylation and HCP-1 staining, which marks kinetochores, were reduced in the absence of either BIR-1 or AIR-2. We propose that BIR-l localizes AIR-2 to chromosomes and perhaps to the spindle midzone, where AIR-2 phosphorylates proteins that affect chromosome behavior and spindle midzone organization. The human BIRP survivin, which is upregulated in tumors, could partially substitute for BIR-1 in C. elegans. Deregulation of bir-l promotes changes in ploidy, suggesting that similar deregulation of mammalian BIRPs may contribute to tumorigenesis.

关键词：秀丽新小杆线虫/遗传学秀丽新小杆线虫/生理学漂亮新小杆线虫蛋白质类细胞周期/生理学细胞分裂染色体图染色体/生理学胚胎非哺乳动物/生理学基因蠕虫蠕虫蛋白质类/遗传学蠕虫蛋白质类/代谢凋亡抑制蛋白质类微管相关蛋白质类分子序列数据肿瘤蛋白质类卵母细胞/生理学蛋白质丝氨酸苏氨酸激酶/代谢蛋白质类/代谢精子/生理学动物女(雌)性人类男(雄)性

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A conserved transcription motif suggesting functional parallels between Caenorhabditis elegans SKN-1 and Cap'n'Collar-related basic leucine zipper proteins

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JOURNAL OF BIOLOGICAL CHEMISTRY 2000年第29期275卷 22166-22171页

作者： Walker, AK See, R Batchelder, C Kophengnavong, T Gronniger, JT Shi, Y Blackwell, TK Harvard Univ Sch Med Ctr Blood Res Boston MA 02115 USA Harvard Univ Sch Med Dept Pathol Boston MA 02115 USA

In Caenorhabditis elegans, the predicted transcription factor SKN-1 is required for embryonic endodermal and mesodermal specification and for maintaining differentiated intestinal cells post-embryonically. The SKN-1 DNA-binding region is related to the Cap'n'Collar (CNC) family of basic leucine zipper proteins, but uniquely, SKN-1 binds DNA as a monomer. CNC proteins are absent in C, elegans, however;and their involvement in the endoderm and mesoderm suggests some functional parallels to SKN-1, Using a cell culture assay, we show that SKN-1 induces transcription and contains three potent activation domains. The functional core of one domain is a short motif, the DIDLID element, which is highly conserved in a subgroup of vertebrate CNC proteins. The DIDLID element is important for SKN-1-driven transcription, suggesting a likely significance in other CNC proteins. SKN-1 binds to and activates transcription through the p300/cAMP-rrespossvv element-binding protein-binding protein (CBP) coactivator, supporting the genetic prediction that SKN-1 recruits the C, elegans p300/CBP ortholog, CBP-1, The DIDLID element appears to act independently of p300/CBP, however, suggesting a distinct conserved target. The evolutionarily preservation of the DIDLID transcriptional element supports the model that SKN-1 and some CNC proteins interact with analogous cofactors and may have preserved some similar functions despite having divergent DNA-binding domains.

关键词：新小杆线虫漂亮/遗传学漂亮新小杆线虫蛋白质类 DNA结合蛋白质类/遗传学果蝇蛋白质类蠕虫蛋白质类/遗传学亮氨酸拉链/遗传学阻遏蛋白质类/遗传学转录因子/遗传学转录遗传动物

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Identification and characterization of a dimerization domain in CED-6, an adapter protein involved in engulfment of apoptotic cells

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JOURNAL OF BIOLOGICAL CHEMISTRY 2000年第13期275卷 9542-9549页

作者： Su, HP Brugnera, E Van Criekinge, W Smits, E Hengartner, M Bogaert, T Ravichandran, KS Univ Virginia Beirne Carter Ctr Immunol Res Charlottesville VA 22908 USA Univ Virginia Dept Microbiol Charlottesville VA 22908 USA DEVGEN NV B-9052 Ghent Belgium Cold Spring Harbor Lab Cold Spring Harbor NY 11724 USA

Phagocytosis of apoptotic cells is a key step in the completion of programmed cell death that occurs throughout life in multicellular organisms. The molecular events involved in clearance of apoptotic cells are just beginning to be elucidated. Recently, CED-6, an adapter protein involved in engulfment has been cloned in Caenorhabditis elegans and in humans. CED-6 is composed of a phosphotyrosine-binding (PTB) domain and a proline-rich C-terminal domain with no apparent catalytic domain. Since PTB domains, originally identified in Shc, mediate intracellular signaling downstream of cell surface receptors, CED-6 has also been proposed to mediate intracellular signals leading to engulfment. In this report, we demonstrate that CED-6 dimerizes through a leucine zipper domain that is immediately adjacent to the PTB domain, Several lines of evidence based on co-immunoprecipitation studies, yeast two-hybrid assays, and gel filtration studies suggest that CED-B exists as a dimer in vivo. Through mutational analyses, we show that the leucine zipper is necessary and sufficient for CED-6 dimerization and that this dimerization is conserved among C. elegans, rodent, and human CED-6 proteins. We propose that dimerization may have unique implications for ligand binding via CED-6 and its function during the phagocytosis of apoptotic cells.

关键词：氨基酸序列细胞凋亡碱基序列 COS细胞秀丽新小杆线虫/代谢漂亮新小杆线虫蛋白质类仓鼠亚科 DNA引物二聚作用蠕虫蛋白质类/化学蠕虫蛋白质类/代谢亮氨酸拉链分子序列数据磷蛋白类/化学磷蛋白类/代谢序列同源性氨基酸信号传导种特异性动物人类

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Identification and characterization of a novel protein from sertoli cells, PASS1, that associates with mammalian small stress protein hsp27

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JOURNAL OF BIOLOGICAL CHEMISTRY 2000年第25期275卷 18724-18731页

作者： Liu, CH Gilmont, RR Benndorf, R Welsh, MJ Univ Michigan Sch Med Dept Cell & Dev Biol Ann Arbor MI 48109 USA Univ Michigan Sch Med Dept Plast & Reconstruct Surg Ann Arbor MI 48109 USA

hsp27 is involved in development of tolerance to stress, possibly by its involvement in molecular chaperoning, maintenance of glutathione status, and/or modulation of microfilament structure and function. We hypothesize that hsp27 function depends on specific association with other proteins. To discover proteins that associate with hsp27, we made a differentiated rat Sertoli cell cDNA expression library and screened it using the yeast two-hybrid system. We obtained a cDNA coding for a novel protein of 428 amino acids that we have named PASS1 (protein associated with Small stress proteins 1). BLAST searches did not reveal major similarity of PASS1 to any known protein, but the cDNA sequence matched several mouse EST clones and shares 34% homology with a Caenorhabditis elegans genomic sequence. In vitro, bacterially expressed glutathione S-transferase-PASS1 fusion protein bound to hsp27, and hsp27 was co-immunoprecipitated with c-Myc-tagged PASS1 overexpressed in several cell lines. The region of PASS1 responsible for association with hsp27 was identified as existing predominantly between amino acids 108 and 208 of PASS1, Northern hybridization and Western blot analysis demonstrated that PASS1 is expressed in several tissues, with the highest expression occurring in testis, primarily in Sertoli cells. The presence of a 1.4-kilobase PASS1 mRNA in kidney as well as the 1.8-kilobase mRNA seen in other tissues suggests that alternate splicing may occur in this organ. Ectopic expression of PASS1 in two cultured cell lines was observed to inhibit the ability of hsp27 to protect cells against heat shock, indicating that PASS1 does interact with hsp27 in the live cell.

关键词：氨基酸序列碱基序列漂亮新小杆线虫蛋白质类载体蛋白质类/遗传学载体蛋白质类/代谢细胞系克隆分子 DNA 互补热休克蛋白质类热休克反应/遗传学分子序列数据肿瘤蛋白质类/代谢蛋白质结合塞尔托利细胞/代谢动物男(雄)性小鼠大鼠

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A global profile of germline gene expression in C-elegans

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MOLECULAR CELL 2000年第3期6卷 605-616页

作者： Reinke, V Smith, HE Nance, J Wang, J Van Doren, C Begley, R Jones, SJM Davis, EB Scherer, S Ward, S Kim, SK Univ Arizona Dept Mol & Cellular Biol Tucson AZ 85721 USA Stanford Univ Med Ctr Sch Med Dept Dev Biol Stanford CA 94305 USA Rosetta Inpharmat Kirkland WA 98034 USA British Columbia Canc Res Ctr Genome Sequence Ctr Vancouver BC V5Z 1L3 Canada

We used DNA microarrays to profile gene expression patterns in the C. elegans germline and identified 1416 germline-enriched transcripts that define three groups. The sperm-enriched group contains an unusually large number of protein kinases and phosphatases. The oocyte-enriched group includes potentially new components of embryonic signaling pathways. The germline-intrinsic group, defined as genes expressed similarly in germlines making only sperm or only oocytes, contains a family of piwi-related genes that may be important for stem cell proliferation. Finally, examination of the chromosomal location of germline transcripts revealed that sperm-enriched and germline-intrinsic genes are nearly absent from the X chromosome, but oocyte-enriched genes are not.

关键词： Argonaute蛋白质类秀丽新小杆线虫/遗传学漂亮新小杆线虫蛋白质类细胞周期蛋白质类/遗传学细胞支架蛋白质类/遗传学果蝇蛋白质类基因表达谱基因表达调控发育期蠕虫蛋白质类/遗传学膜蛋白质类/遗传学卵母细胞/生理学蛋白质类/遗传学 RNA 信使/遗传学 RNA诱导沉默复合物受体 Notch 精子发生/遗传学精子/生理学 X染色体动物男(雄)性

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The TBP-like factor CeTLF is required to activate RNA polymerase II transcription during C-elegans embryogenesis

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MOLECULAR CELL 2000年第3期6卷 705-713页

作者： Kaltenbach, L Horner, MA Rothman, JH Mango, SE Univ Utah Huntsman Canc Inst Ctr Children Salt Lake City UT 84112 USA Univ Utah Dept Oncol Sci Salt Lake City UT 84112 USA Univ Calif Santa Barbara Dept Mol Cellular & Dev Biol Santa Barbara CA 93106 USA

Metazoans possess two TATA-binding protein homologs, the general transcription factor TBP and a related factor called TLF. Four models have been proposed for the role of TLF in RNA polymerase II (Pol Il) transcription: (1) TLF and TBP function redundantly, (2) TLF antagonizes TBP, (3) TLF is a tissue-specific TBP, or (4) TLF and TBP have distinct activities. Here we report that CeTLF is required to express a subset of Pol II genes and associates with at least one of these genes in vivo. CeTLF is also necessary to establish bulk transcription during early embryogenesis. Since CeTLF and CeTBP are expressed at comparable levels in the same cells, these findings suggest CeTLF performs a unique function in activating Pol II transcription distinct from that of CeTBP.

关键词：氨基酸序列秀丽新小杆线虫/遗传学漂亮新小杆线虫蛋白质类 DNA结合蛋白质类/遗传学 DNA结合蛋白质类/代谢胚胎非哺乳动物/生理学基因表达调控发育期分子序列数据表型启动区遗传/生理学 RNA聚合酶Ⅱ/代谢 RNA 信使/分析 TATA盒结合蛋白样蛋白质类转录因子/遗传学转录因子/代谢转录激活/生理学动物

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Disruption of the CED-9•CED-4 complex by EGL-1 is a critical step for programmed cell death in Caenorhabditis elegans

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JOURNAL OF BIOLOGICAL CHEMISTRY 2000年第35期275卷 27205-27211页

作者： del Peso, L González, VM Inohara, N Ellis, RE Núñez, G Univ Michigan Dept Pathol Ann Arbor MI 48109 USA Univ Michigan Ctr Comprehens Canc Ann Arbor MI 48109 USA Univ Michigan Dept Biol Ann Arbor MI 48109 USA

In the nematode Caenorhabditis elegans, the apoptotic machinery is composed of four basic elements: the caspase CED-3, the Apaf-1 homologue CED-4, and the Bcl-2 family members CED-9 and EGL-1. The ced-9(n1950) gain-of-function mutation prevents most, if not all, somatic cell deaths in C. elegans. It encodes a CED-9 protein with a glycine-to-glutamate substitution at position 169, which is located within the highly conserved Bcl-2 homology 1 domain, We performed biochemical analyses with the CED-9G169E protein to gain insight into the mechanism of programmed cell death, We find that CED-9G169E retains the ability to bind both EGL-1 and CED-4, although its affinity for EGL-1 is reduced. In contrast to the behavior of wild-type CED-9, the interaction between CED-9G169E and CED-4 is not disrupted by expression of EGL-1. Furthermore, CED-4 and CED-9G169E co-localizes with EGL-1 to the mitochondria in mammalian cells, and expression of EGL-1 does not induce translocation of CED-4 to the cytosol, Finally, the ability of EGL-1 to promote apoptosis is impaired by the replacement of wild-type CED-9 with CED-9G169E, and this effect is correlated with the inability of EGL-1 to induce the displacement of CED-4 from the CED-9 CED-4 complex. These studies suggest that the release of CED-4 from the ***-4 complex is a necessary step for induction of programmed cell death in C. elegans.

关键词：氨基酸序列细胞凋亡/遗传学凋亡调节蛋白质类新小杆线虫漂亮/细胞学新小杆线虫漂亮/代谢漂亮新小杆线虫蛋白质类钙结合蛋白质类/化学钙结合蛋白质类/代谢蠕虫蛋白质类/化学蠕虫蛋白质类/遗传学蠕虫蛋白质类/代谢分子序列数据突变蛋白质结合原癌基因蛋白质类/化学原癌基因蛋白质类/遗传学原癌基因蛋白质类/代谢阻遏蛋白质类/代谢序列同源性氨基酸动物

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