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Greasing the protein biosynthesis machinery of photoreceptor neurons: Role for postprenylation processing of proteins. 润滑光感受器神经元的蛋白质生物合成机制:蛋白质后烯酰化加工的作用。
Cellular logistics Pub Date : 2012-01-01 DOI: 10.4161/cl.19804
Jeffrey R Christiansen, Visvanathan Ramamurthy
{"title":"Greasing the protein biosynthesis machinery of photoreceptor neurons: Role for postprenylation processing of proteins.","authors":"Jeffrey R Christiansen,&nbsp;Visvanathan Ramamurthy","doi":"10.4161/cl.19804","DOIUrl":"https://doi.org/10.4161/cl.19804","url":null,"abstract":"<p><p>Daily phagocytosis of outer segments (OS) places extraordinary demands on protein biosynthesis and trafficking in photoreceptor neurons. While the members and roles of the phototransduction pathway in the OS are well characterized, details about protein trafficking are just beginning to emerge. Phosphodiesterase6 (PDE6), the effector enzyme in phototransduction cascade, serves as an example of the steps multimeric proteins must pass through to achieve their functional state in the OS. Genetic model systems have recently provided snapshots of various steps in the pathway, as experimental difficulties such as an inability to maintain ciliated photoreceptor outer segments or express functional PDE6 holoenzyme in vitro necessitate in vivo studies. We will highlight the significant findings, their implications to blinding diseases, as well as discuss the gaps requiring further investigation.</p>","PeriodicalId":72547,"journal":{"name":"Cellular logistics","volume":" ","pages":"15-19"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4161/cl.19804","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30653312","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 5
AP180 and CALM: Dedicated endocytic adaptors for the retrieval of synaptobrevin 2 at synapses. AP180和CALM:专用的内吞适配器，用于检索突触上的突触短肽2。
Cellular logistics Pub Date : 2011-07-01 DOI: 10.4161/cl.1.4.18897
Seong Joo Koo, Dmytro Puchkov, Volker Haucke
{"title":"AP180 and CALM: Dedicated endocytic adaptors for the retrieval of synaptobrevin 2 at synapses.","authors":"Seong Joo Koo,&nbsp;Dmytro Puchkov,&nbsp;Volker Haucke","doi":"10.4161/cl.1.4.18897","DOIUrl":"https://doi.org/10.4161/cl.1.4.18897","url":null,"abstract":"<p><p>Communication between neurons largely occurs at chemical synapses by conversion of electric to chemical signals. Chemical neurotransmission involves the action potential-driven release of neurotransmitters from synaptic vesicles (SVs) at presynaptic nerve terminals. Fusion of SVs is driven by SNARE complex formation comprising synaptobrevin 2 on the SV membrane and syntaxin 1A and SNAP-25 on the plasma membrane. In order to maintain neurotransmission during repetitive stimulation and to prevent expansion of the presynaptic plasma membrane, exocytic SV fusion needs to be balanced by compensatory retrieval of SV components to regenerate functional vesicles. Our recent work has unraveled a mechanism by which the R-SNARE synaptobrevin 2, the most abundant SV protein and an essential player for exocytic fusion, is recycled from the presynaptic membrane. The SNARE motif of synaptobrevin 2 is directly recognized by the ANTH domains of AP180 and CALM, monomeric endocytic adaptors for clathrin-mediated endocytosis. Given that key residues involved in synaptobrevin 2-ANTH domain complex formation are also essential for SNARE assembly, we propose that disassembly of SNARE complexes is a prerequisite for synaptobrevin 2 retrieval, thereby preventing endocytic mis-sorting of the plasma membrane Q-SNAREs syntaxin 1A and SNAP-25. It is tempting to speculate that perturbed synaptobrevin 2 recycling caused by reduction of CALM or AP180 levels may lead to disease as suggested by the genetic association of ANTH domain proteins with neurodegenerative disorders.</p>","PeriodicalId":72547,"journal":{"name":"Cellular logistics","volume":"1 4","pages":"168-172"},"PeriodicalIF":0.0,"publicationDate":"2011-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4161/cl.1.4.18897","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30416343","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 13
ThANKs for the repeat: Intracellular pathogens exploit a common eukaryotic domain. 感谢重复:细胞内病原体利用一个共同的真核结构域。
Cellular logistics Pub Date : 2011-07-01 DOI: 10.4161/cl.1.4.18738
Daniel E Voth
{"title":"ThANKs for the repeat: Intracellular pathogens exploit a common eukaryotic domain.","authors":"Daniel E Voth","doi":"10.4161/cl.1.4.18738","DOIUrl":"https://doi.org/10.4161/cl.1.4.18738","url":null,"abstract":"<p><p>Bacterial pathogens are renowned cell biologists that subvert detrimental host responses by manipulating eukaryotic protein function. A select group of pathogens use a specialized type IV secretion system (T4SS) as a conduit to deliver an arsenal of proteins into the host cytosol where they interact with host proteins. The translocated \"effectors\" have garnered increased attention because they uncover novel aspects of host-pathogen interactions at the subcellular level. This review presents a group of effectors termed Anks that possess eukaryotic-like ankyrin repeat domains that mediate proteinprotein interactions and are critical for effector function. Interestingly, most known prokaryotic Anks are produced by bacteria that devote much of their time to replicating inside eukaryotic cells. Ank proteins represent a fascinating and versatile family of effectors exploited by bacterial pathogens and are proving useful as tools to study eukaryotic cell biology.</p>","PeriodicalId":72547,"journal":{"name":"Cellular logistics","volume":"1 4","pages":"128-132"},"PeriodicalIF":0.0,"publicationDate":"2011-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4161/cl.1.4.18738","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30415463","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 13
Dual function of Sec16B: Endoplasmic reticulum-derived protein secretion and peroxisome biogenesis in mammalian cells. Sec16B的双重功能:哺乳动物细胞内质网源性蛋白分泌和过氧化物酶体的生物发生。
Cellular logistics Pub Date : 2011-07-01 DOI: 10.4161/cl.1.4.18341
Katsuko Tani, Mitsuo Tagaya, Shusuke Yonekawa, Takashi Baba
{"title":"Dual function of Sec16B: Endoplasmic reticulum-derived protein secretion and peroxisome biogenesis in mammalian cells.","authors":"Katsuko Tani,&nbsp;Mitsuo Tagaya,&nbsp;Shusuke Yonekawa,&nbsp;Takashi Baba","doi":"10.4161/cl.1.4.18341","DOIUrl":"https://doi.org/10.4161/cl.1.4.18341","url":null,"abstract":"<p><p>The origin of peroxisomes has long been disputed. However, recent evidence suggests that peroxisomes can be formed de novo from the endoplasmic reticulum (ER) in yeast and higher eukaryotes. Sec16A and Sec16B, mammalian orthologs of yeast Sec16, are scaffold proteins that organize ER exit sites by interacting with COPII components. We recently demonstrated that Sec16B, but not Sec16A, regulates the transport of peroxisomal biogenesis factors from the ER to peroxisomes in mammalian cells. The C-terminal region of Sec16B, which is not conserved in Sec16A, is required for this function. The data suggest that Sec16B in ER areas other than ER exit sites plays this role. Our findings provide an unexpected connection between at least part of the COPII machinery and the formation of preperoxisomal vesicles at the ER, and offer an explanation of how secretory and peroxisomal trafficking from the ER are distinguished.</p>","PeriodicalId":72547,"journal":{"name":"Cellular logistics","volume":"1 4","pages":"164-167"},"PeriodicalIF":0.0,"publicationDate":"2011-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4161/cl.1.4.18341","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30415467","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 10
Rab1b regulates COPI and COPII dynamics in mammalian cells. Rab1b调控哺乳动物细胞中COPI和COPII的动态。
Cellular logistics Pub Date : 2011-07-01 DOI: 10.4161/cl.1.4.18221
Iris A García, Hernán E Martinez, Cecilia Alvarez
{"title":"Rab1b regulates COPI and COPII dynamics in mammalian cells.","authors":"Iris A García,&nbsp;Hernán E Martinez,&nbsp;Cecilia Alvarez","doi":"10.4161/cl.1.4.18221","DOIUrl":"https://doi.org/10.4161/cl.1.4.18221","url":null,"abstract":"<p><p>Rabs GTPases are key regulatory factors that specifically associate to organelles that integrate membrane transport pathways. Rabs, through their interactions with diverse effector proteins, regulate the formation, movement, tethering and fusion of transport carriers (vesicles and/or tubules). The mammalian Rab1b GTPase is required for ER to Golgi transport and interacts with multiple effectors localized at the ER-Golgi interface. Here, we focus on interactions between Rab1b and effectors that play essential roles in COPII and COPI vesicle formation/function. Based on evidence to date, we propose a model of Rab1b action at the ER exit sites.</p>","PeriodicalId":72547,"journal":{"name":"Cellular logistics","volume":"1 4","pages":"159-163"},"PeriodicalIF":0.0,"publicationDate":"2011-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4161/cl.1.4.18221","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30415466","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 14
ArfGAP1 promotes COPI vesicle formation by facilitating coatomer polymerization. ArfGAP1 通过促进衣壳聚合物聚合来促进 COPI 囊泡的形成。
Cellular logistics Pub Date : 2011-07-01 DOI: 10.4161/cl.1.4.18896
Yoko Shiba, Ruibai Luo, Jenny E Hinshaw, Tomasz Szul, Ryo Hayashi, Elizabeth Sztul, Kunio Nagashima, Ulrich Baxa, Paul A Randazzo
{"title":"ArfGAP1 promotes COPI vesicle formation by facilitating coatomer polymerization.","authors":"Yoko Shiba, Ruibai Luo, Jenny E Hinshaw, Tomasz Szul, Ryo Hayashi, Elizabeth Sztul, Kunio Nagashima, Ulrich Baxa, Paul A Randazzo","doi":"10.4161/cl.1.4.18896","DOIUrl":"10.4161/cl.1.4.18896","url":null,"abstract":"<p><p>The role of ArfGAP1 in COPI vesicle biogenesis has been controversial. In work using isolated Golgi membranes, ArfGAP1 was found to promote COPI vesicle formation. In contrast, in studies using large unilamellar vesicles (LUVs) as model membranes, ArfGAP1 functioned as an uncoating factor inhibiting COPI vesicle formation. We set out to discriminate between these models. First, we reexamined the effect of ArfGAP1 on LUVs. We found that ArfGAP1 increased the efficiency of coatomer-induced deformation of LUVs. Second, ArfGAP1 and peptides from cargo facilitated self-assembly of coatomer into spherical structures in the absence of membranes, reminiscent of clathrin self-assembly. Third, in vivo, ArfGAP1 overexpression induced the accumulation of vesicles and allowed normal trafficking of a COPI cargo. Taken together, these data support the model in which ArfGAP1 promotes COPI vesicle formation and membrane traffic and identify a function for ArfGAP1 in the assembly of coatomer into COPI.</p>","PeriodicalId":72547,"journal":{"name":"Cellular logistics","volume":"1 4","pages":"139-154"},"PeriodicalIF":0.0,"publicationDate":"2011-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3265926/pdf/cl0104_0139.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30416344","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Catch and release: Rab1 exploitation by Legionella pneumophila. 嗜肺军团菌对Rab1的捕获与释放。
Cellular logistics Pub Date : 2011-07-01 DOI: 10.4161/cl.1.4.18933
Matthias P Machner, Yang Chen
{"title":"Catch and release: Rab1 exploitation by Legionella pneumophila.","authors":"Matthias P Machner,&nbsp;Yang Chen","doi":"10.4161/cl.1.4.18933","DOIUrl":"https://doi.org/10.4161/cl.1.4.18933","url":null,"abstract":"<p><p>The intracellular pathogen Legionella pneumophila exploits host cell vesicular transport by manipulating the activity of the small GTPase Rab1. Bacterial proteins, so called effectors, that are delivered into the infected cell play a key role in this process. Here, we summarize recent developments in our quest to understand the molecular function of these effectors, and describe how L. pneumophila employs post-translational modification in a reversible manner to manipulate the activity of Rab1 on its vacuole.</p>","PeriodicalId":72547,"journal":{"name":"Cellular logistics","volume":"1 4","pages":"133-138"},"PeriodicalIF":0.0,"publicationDate":"2011-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4161/cl.1.4.18933","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30415464","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 4
A note from the Editor-in-Chief. 总编辑的留言。
Cellular logistics Pub Date : 2011-07-01 DOI: 10.4161/cl.1.4.18934
Nava Segev
{"title":"A note from the Editor-in-Chief.","authors":"Nava Segev","doi":"10.4161/cl.1.4.18934","DOIUrl":"https://doi.org/10.4161/cl.1.4.18934","url":null,"abstract":"","PeriodicalId":72547,"journal":{"name":"Cellular logistics","volume":"1 4","pages":"119"},"PeriodicalIF":0.0,"publicationDate":"2011-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4161/cl.1.4.18934","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30415460","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Take it and release it: The use of the Rab1 small GTPase at a bacterium's will. 吸收并释放:细菌可以随意使用Rab1小GTPase。
Cellular logistics Pub Date : 2011-07-01 DOI: 10.4161/cl.1.4.17870
Yunhao Tan, Zhao-Qing Luo
{"title":"Take it and release it: The use of the Rab1 small GTPase at a bacterium's will.","authors":"Yunhao Tan,&nbsp;Zhao-Qing Luo","doi":"10.4161/cl.1.4.17870","DOIUrl":"https://doi.org/10.4161/cl.1.4.17870","url":null,"abstract":"<p><p>Successful pathogens are equipped to exploit the signaling pathways of their host cell to establish a niche conducive for their survival and proliferation. One emerging example is the modulation of the small GTPase Rab1 by virulence factors of the intracellular pathogen Legionella pneumophila. Besides proteins that mimic host regulatory factors involved in controlling Rab1 activity, this bacterium temporally locks this small GTPase in its active form by AMPylation. Efficient release of Rab1 from the bacterial phagosome requires deAMPylation prior to being inactivated by the bacterial GAP protein LepB. Whether Rab activity is similarly regulated under native condition is unknown, but it is clear that virulence factors from pathogens can be invaluable tools in dissecting the intricacy of host cellular processes.</p>","PeriodicalId":72547,"journal":{"name":"Cellular logistics","volume":"1 4","pages":"125-127"},"PeriodicalIF":0.0,"publicationDate":"2011-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4161/cl.1.4.17870","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30415462","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 4
Bringing host-cell takeover by pathogenic bacteria to center stage. 使宿主细胞被致病菌接管成为焦点。
Cellular logistics Pub Date : 2011-07-01 DOI: 10.4161/cl.1.4.18984
Ron Dubreuil, Nava Segev
{"title":"Bringing host-cell takeover by pathogenic bacteria to center stage.","authors":"Ron Dubreuil,&nbsp;Nava Segev","doi":"10.4161/cl.1.4.18984","DOIUrl":"https://doi.org/10.4161/cl.1.4.18984","url":null,"abstract":"<p><p>Intracellular pathogenic bacteria contrive processes in their host cell to create a niche for their own reproduction. One way that has emerged by which bacteria do that is delivery of secreted virulence factors, SVFs, to the cytoplasm of the host cells using the bacterial type IV secretion system, T4SS. These SVFs modulate the activity of their target host proteins, which in turn control key cellular processes. A major mechanism for the evolution of SVFs that modulate targets that do not exist in the bacterial kingdom is horizontal gene transfer. Recently, a number of bacterial SVFs were shown to act on two types of targets in host cells. First, a group of several SVFs modulate the activity and localization of one protein: Rab1 GTPase, a key regulator of intracellular trafficking. Second, ankyrin repeats-containing SVFs, referred to by microbiologists as Anks, interact with various binding proteins, which in turn regulate a myriad of cellular processes, including apoptosis. Modulation of trafficking and apoptosis are two examples of how invading bacteria takeover their host phagocyte, which instead of destroying the bacteria becomes a factory for its reproduction.</p>","PeriodicalId":72547,"journal":{"name":"Cellular logistics","volume":"1 4","pages":"120-124"},"PeriodicalIF":0.0,"publicationDate":"2011-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4161/cl.1.4.18984","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30415461","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 4
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