Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
33
pubmed:dateCreated
2002-8-12
pubmed:abstractText
Autophagy is a catabolic membrane-trafficking mechanism involved in cell maintenance and development. Most components of autophagy also function in the cytoplasm to vacuole targeting (Cvt) pathway, a constitutive biosynthetic pathway required for the transport of aminopeptidase I (Ape1). The protein components of autophagy and the Cvt pathway include a putative complex composed of Apg1 kinase and several interacting proteins that are specific for either the Cvt pathway or autophagy. A second required complex includes a phosphatidylinositol (PtdIns) 3-kinase and associated proteins that are involved in its activation and localization. The majority of proteins required for the Cvt and autophagy pathways localize to a perivacuolar pre-autophagosomal structure. We show that the Cvt13 and Cvt20 proteins are required for transport of precursor Ape1 through the Cvt pathway. Both proteins contain phox homology domains that bind PtdIns(3)P and are necessary for membrane localization to the pre-autophagosomal structure. Functional phox homology domains are required for Cvt pathway function. Cvt13 and Cvt20 interact with each other and with an autophagy-specific protein, Apg17, that interacts with Apg1 kinase. These results provide the first functional connection between the Apg1 and PtdIns 3-kinase complexes. The data suggest a role for PtdIns(3)P in the Cvt pathway and demonstrate that this lipid is required at the pre-autophagosomal structure.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-10233148, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-10432293, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-10547367, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-10688190, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-10804463, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-10837477, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-10966461, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-10995454, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-11038174, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-11086004, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-11100732, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-11149920, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-11157979, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-11309418, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-11382760, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-11430817, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-11433291, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-11433300, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-11439176, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-11489210, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-11489916, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-11557775, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-11675395, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-11689437, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-11729306, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-1400574, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-2676517, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-3062374, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-7011403, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-7741731, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-8385367, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-8387919, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-8557740, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-8663607, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-8885233, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-8901576, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-9214379, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-9224892, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-9224897, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-9412464, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-9710615, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-9717241, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-9763421, http://linkedlifedata.com/resource/pubmed/commentcorrection/12048214-9819414
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
277
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
30198-207
pubmed:dateRevised
2011-9-26
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Cooperative binding of the cytoplasm to vacuole targeting pathway proteins, Cvt13 and Cvt20, to phosphatidylinositol 3-phosphate at the pre-autophagosomal structure is required for selective autophagy.
pubmed:affiliation
Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109, USA.
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