001     141325
005     20240321220937.0
024 7 _ |a 10.1083/jcb.200912082
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024 7 _ |a pmid:20548102
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024 7 _ |a pmc:PMC2886346
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024 7 _ |a 0021-9525
|2 ISSN
024 7 _ |a 0095-9901
|2 ISSN
024 7 _ |a 1540-8140
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024 7 _ |a 2327-7440
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024 7 _ |a altmetric:131567
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037 _ _ |a DZNE-2020-07647
041 _ _ |a English
082 _ _ |a 570
100 1 _ |a Farhan, Hesso
|b 0
245 _ _ |a MAPK signaling to the early secretory pathway revealed by kinase/phosphatase functional screening.
260 _ _ |a New York, NY
|c 2010
|b Rockefeller Univ. Press
264 _ 1 |3 online
|2 Crossref
|b Rockefeller University Press
|c 2010-06-14
264 _ 1 |3 print
|2 Crossref
|b Rockefeller University Press
|c 2010-06-14
336 7 _ |a article
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336 7 _ |a Journal Article
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336 7 _ |a ARTICLE
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336 7 _ |a Journal Article
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520 _ _ |a To what extent the secretory pathway is regulated by cellular signaling is unknown. In this study, we used RNA interference to explore the function of human kinases and phosphatases in controlling the organization of and trafficking within the secretory pathway. We identified 122 kinases/phosphatases that affect endoplasmic reticulum (ER) export, ER exit sites (ERESs), and/or the Golgi apparatus. Numerous kinases/phosphatases regulate the number of ERESs and ER to Golgi protein trafficking. Among the pathways identified, the Raf-MEK (MAPK/ERK [extracellular signal-regulated kinase] kinase)-ERK cascade, including its regulatory proteins CNK1 (connector enhancer of the kinase suppressor of Ras-1) and neurofibromin, controls the number of ERESs via ERK2, which targets Sec16, a key regulator of ERESs and COPII (coat protein II) vesicle biogenesis. Our analysis reveals an unanticipated complexity of kinase/phosphatase-mediated regulation of the secretory pathway, uncovering a link between growth factor signaling and ER export.
536 _ _ |a 342 - Disease Mechanisms and Model Systems (POF3-342)
|0 G:(DE-HGF)POF3-342
|c POF3-342
|f POF III
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588 _ _ |a Dataset connected to CrossRef, PubMed,
650 _ 7 |a LMAN1 protein, human
|2 NLM Chemicals
650 _ 7 |a Mannose-Binding Lectins
|2 NLM Chemicals
650 _ 7 |a Membrane Proteins
|2 NLM Chemicals
650 _ 7 |a RNA, Small Interfering
|2 NLM Chemicals
650 _ 7 |a Vesicular Transport Proteins
|2 NLM Chemicals
650 _ 7 |a Phosphotransferases
|0 EC 2.7.-
|2 NLM Chemicals
650 _ 7 |a Mitogen-Activated Protein Kinases
|0 EC 2.7.11.24
|2 NLM Chemicals
650 _ 7 |a Phosphoric Monoester Hydrolases
|0 EC 3.1.3.2
|2 NLM Chemicals
650 _ 2 |a Animals
|2 MeSH
650 _ 2 |a COP-Coated Vesicles: metabolism
|2 MeSH
650 _ 2 |a Databases, Factual
|2 MeSH
650 _ 2 |a Endoplasmic Reticulum: metabolism
|2 MeSH
650 _ 2 |a Fluorescence Recovery After Photobleaching
|2 MeSH
650 _ 2 |a Golgi Apparatus: metabolism
|2 MeSH
650 _ 2 |a HeLa Cells
|2 MeSH
650 _ 2 |a Humans
|2 MeSH
650 _ 2 |a MAP Kinase Signaling System: physiology
|2 MeSH
650 _ 2 |a Mannose-Binding Lectins: genetics
|2 MeSH
650 _ 2 |a Mannose-Binding Lectins: metabolism
|2 MeSH
650 _ 2 |a Membrane Proteins: genetics
|2 MeSH
650 _ 2 |a Membrane Proteins: metabolism
|2 MeSH
650 _ 2 |a Mitogen-Activated Protein Kinases: genetics
|2 MeSH
650 _ 2 |a Mitogen-Activated Protein Kinases: metabolism
|2 MeSH
650 _ 2 |a Phosphoric Monoester Hydrolases: metabolism
|2 MeSH
650 _ 2 |a Phosphotransferases: metabolism
|2 MeSH
650 _ 2 |a RNA Interference
|2 MeSH
650 _ 2 |a RNA, Small Interfering: genetics
|2 MeSH
650 _ 2 |a RNA, Small Interfering: metabolism
|2 MeSH
650 _ 2 |a Secretory Pathway: physiology
|2 MeSH
650 _ 2 |a Vesicular Transport Proteins: genetics
|2 MeSH
650 _ 2 |a Vesicular Transport Proteins: metabolism
|2 MeSH
700 1 _ |a Wendeler, Markus W
|b 1
700 1 _ |a Mitrovic, Sandra
|b 2
700 1 _ |a Fava, Eugenio
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700 1 _ |a Silberberg, Yael
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700 1 _ |a Sharan, Roded
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700 1 _ |a Zerial, Marino
|b 6
700 1 _ |a Hauri, Hans-Peter
|0 P:(DE-HGF)0
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773 1 8 |a 10.1083/jcb.200912082
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|t The Journal of Cell Biology
|v 189
|y 2010
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773 _ _ |a 10.1083/jcb.200912082
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910 1 _ |a Deutsches Zentrum für Neurodegenerative Erkrankungen
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LibraryCollectionCLSMajorCLSMinorLanguageAuthor
Marc 21