Schu, Peter Valentin

[["dc.bibliographiccitation.journal","European Journal of Cell Biology"],["dc.bibliographiccitation.volume","85"],["dc.contributor.author","Benkert, T. C."],["dc.contributor.author","Rekha, P. N."],["dc.contributor.author","Schu, P. V."],["dc.date.accessioned","2018-11-07T10:11:08Z"],["dc.date.available","2018-11-07T10:11:08Z"],["dc.date.issued","2006"],["dc.format.extent","32"],["dc.identifier.isi","000237127500057"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/39991"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Gmbh, Urban & Fischer Verlag"],["dc.publisher.place","Jena"],["dc.relation.conference","29th Annual Meeting of the German Society for Cell Biology"],["dc.relation.eventlocation","Braunschweig, GERMANY"],["dc.relation.issn","0171-9335"],["dc.title","Suvia1p required for dodecamerization and transport of vacuolar aminopeptidase I"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","142"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Molecular Neurobiology"],["dc.bibliographiccitation.lastpage","161"],["dc.bibliographiccitation.volume","52"],["dc.contributor.author","Kratzke, Manuel"],["dc.contributor.author","Candiello, Ermes"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Schu, Peter"],["dc.date.accessioned","2018-11-07T09:54:05Z"],["dc.date.available","2018-11-07T09:54:05Z"],["dc.date.issued","2015"],["dc.description.abstract","Adaptor protein (AP)-1/sigma 1B(-/-) mice have reduced synaptic-vesicle (SV) recycling and increased endosomes. Mutant mice have impaired spatial memory, and sigma 1B-deficient humans have a severe mental retardation. In order to define these sigma 1B(-/-) 'bulk' endosomes and to determine their functions in SV recycling, we developed a protocol to separate them from the majority of the neuronal endosomes. The sigma 1B(-/-) 'bulk' endosomes proved to be classic early endosomes with an increase in the phospholipid phosphatidylinositol 3-phosphate (PI-3-P), which recruits proteins mediating protein sorting out of early endosomes into different routes. sigma 1B deficiency induced alterations in the endosomal proteome reveals two major functions: SV protein storage and sorting into endolysosomes. Alternative endosomal recycling pathways are not up-regulated, but certain SV proteins are misrouted. Tetraspanins are enriched in sigma 1B(-/-) synaptosomes, but not in their endosomes or in their clathrin-coated-vesicles (CCVs), indicating AP-1/sigma 1B-dependent sorting. Synapses contain also more AP-2 CCV, although it is expected that they contain less due to reduced SV recycling. Coat composition of these AP-2 CCVs is altered, and thus, they represent a subpopulation of AP-2 CCVs. Association of calmodulin-dependent protein kinase (CaMK)-II alpha, -delta and casein kinase (CK)-II alpha with the endosome/SV pool is altered, as well as 14-3-3 eta, indicating changes in specific signalling pathways regulating synaptic plasticity. The accumulation of early endosomes and endocytotic AP-2 CCV indicates the regulation of SV recycling via early endosomes by the interdependent regulation of AP-2-mediated endocytosis and AP-1/sigma 1B-mediated SV reformation."],["dc.description.sponsorship","DFG [Schu 802/3-1, 802/3-2]"],["dc.identifier.doi","10.1007/s12035-014-8852-0"],["dc.identifier.isi","000358341600014"],["dc.identifier.pmid","25128028"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/36465"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Humana Press Inc"],["dc.relation.issn","1559-1182"],["dc.relation.issn","0893-7648"],["dc.title","AP-1/sigma 1B-Dependent SV Protein Recycling Is Regulated in Early Endosomes and Is Coupled to AP-2 Endocytosis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","10277"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","10283"],["dc.bibliographiccitation.volume","280"],["dc.contributor.author","Kyttala, A."],["dc.contributor.author","Yliannala, K."],["dc.contributor.author","Schu, Peter Valentin"],["dc.contributor.author","Jalanko, A."],["dc.contributor.author","Luzio, J. P."],["dc.date.accessioned","2018-11-07T11:15:49Z"],["dc.date.available","2018-11-07T11:15:49Z"],["dc.date.issued","2005"],["dc.description.abstract","CLN3 is a transmembrane protein with a predominant localization in lysosomes in non-neuronal cells but is also found in endosomes and the synaptic region in neuronal cells. Mutations in the CLN3 gene result in juvenile neuronal ceroid lipofuscinosis or Batten disease, which currently is the most common cause of childhood dementia. We have recently reported that the lysosomal targeting of CLN3 is facilitated by two targeting motifs: a dileucine-type motif in a cytoplasmic loop domain and an unusual motif in the carboxyl-terminal cytoplasmic tail comprising a methionine and a glycine separated by nine amino acids (Kyttala, A., Ihrke, G., Vesa, J., Schell, M. J., and Luzio, J. P. (2004) Mol. Biol. Cell 15, 1313-1323). In the present study, we investigated the pathways and mechanisms of CLN3 sorting using biochemical binding assays and immunofluorescence methods. The dileucine motif of CLN3 bound both AP-1 and AP-3 in vitro, and expression of mutated CLN3 in AP-1- or AP-3-deficient mouse fibroblasts showed that both adaptor complexes are required for sequential sorting of CLN3 via this motif. Our data indicate the involvement of complex sorting machinery in the trafficking of CLN3 and emphasize the diversity of parallel and sequential sorting pathways in the trafficking of membrane proteins."],["dc.identifier.doi","10.1074/jbc.M411862200"],["dc.identifier.isi","000227559600066"],["dc.identifier.pmid","15598649"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/54448"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Biochemistry Molecular Biology Inc"],["dc.relation.issn","0021-9258"],["dc.title","AP-1 and AP-3 facilitate lysosomal targeting of batten disease protein CLN3 via its dileucine motif"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","67"],["dc.bibliographiccitation.lastpage","78"],["dc.bibliographiccitation.seriesnr","451"],["dc.contributor.author","Schu, Peter"],["dc.date.accessioned","2018-11-07T11:19:29Z"],["dc.date.available","2018-11-07T11:19:29Z"],["dc.date.issued","2008"],["dc.description.abstract","Aminopeptidase I is the cargo protein of the cytoplasm-to-vacuole targeting (Cvt), autophagy-like protein-targeting pathway of the yeast Saccharomyces cerevisiae, the nonclassical vacuolar biosynthetic transport route. The second enzyme following this route to the vacuole, a-mannosidase, is also transported by direct binding to the Atg19 receptor and to aminopeptidase I. Aminopepticlase I forms a homododecameric complex, which is synthesized and assembled in the cytoplasm, packed in double-membrane vesicles, and transported to the vacuole. Only the homododecameric complex of aminopeptidase I has exopeptidase activity directed against amino-terminal leucine residues. Enzymatic activity can be determined spectrofluorometrically in homogenates and semi-quantitatively after nondenaturing gel electrophoresis and by yeast colony-overlay assay. This chapter describes the methods to determine aminopeptidase I enzymatic activity used to follow complex assembly and vacuolar transport."],["dc.identifier.doi","10.1016/S0076-6879(08)03206-0"],["dc.identifier.isi","000262255500006"],["dc.identifier.pmid","19185714"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/55293"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Academic Press Inc"],["dc.publisher.place","San diego"],["dc.relation.crisseries","Methods in Enzymology"],["dc.relation.isbn","978-0-12-374548-4"],["dc.relation.ispartof","AUTOPHAGY: LOWER EUKARYOTES AND NON-MAMMALIAN SYSTEMS, PT A"],["dc.relation.ispartofseries","Methods in Enzymology; 451"],["dc.relation.issn","0076-6879"],["dc.title","AMINOPEPTIDASE I ENZYMATIC ACTIVITY"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3477"],["dc.bibliographiccitation.issue","16"],["dc.bibliographiccitation.journal","Journal of Cell Science"],["dc.bibliographiccitation.lastpage","3487"],["dc.bibliographiccitation.volume","127"],["dc.contributor.author","Baltes, Jennifer"],["dc.contributor.author","Larsen, Jakob Vejby"],["dc.contributor.author","Radhakrishnan, Karthikeyan"],["dc.contributor.author","Geumann, Constanze"],["dc.contributor.author","Kratzke, Manuel"],["dc.contributor.author","Petersen, Claus Munck"],["dc.contributor.author","Schu, Peter"],["dc.date.accessioned","2018-11-07T09:36:33Z"],["dc.date.available","2018-11-07T09:36:33Z"],["dc.date.issued","2014"],["dc.description.abstract","Here, we describe altered sorting of sortilin in adipocytes deficient for the sigma 1B-containing AP-1 complex, leading to the inhibition of adipogenesis. The AP-1 complex mediates protein sorting between the trans-Golgi network and endosomes. Vertebrates express three AP1 sigma 1 subunit isoforms - sigma 1A, sigma 1B and sigma 1C (also known as AP1S1, AP1S2 and AP1S3, respectively). sigma 1B-deficient mice display impaired recycling of synaptic vesicles and lipodystrophy. Here, we show that sortilin is overexpressed in adipose tissue from sigma 1B(-/-) mice, and that its overexpression in wild-type cells is sufficient to suppress adipogenesis. sigma 1B-specific binding of sortilin requires the sortilin DxxD-x12-DSxxxL motif. sigma 1B deficiency does not lead to a block of sortilin transport out of a specific organelle, but the fraction that reaches lysosomes is reduced. Sortilin binds to the receptor DLK1, an inhibitor of adipocyte differentiation, and the overexpression of sortilin prevents DLK1 downregulation, leading to enhanced inhibition of adipogenesis. DLK1 and sortilin expression are not increased in the brain tissue of sigma 1B(-/-) mice, although this is the tissue with the highest expression of sigma 1B and sortilin. Thus, adipose-tissue-specific and sigma 1B-dependent routes for the transport of sortilin exist and are involved in the regulation of adipogenesis and adipose-tissue mass."],["dc.identifier.doi","10.1242/jcs.146886"],["dc.identifier.isi","000341180000008"],["dc.identifier.pmid","24928897"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/32644"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Company Of Biologists Ltd"],["dc.relation.issn","1477-9137"],["dc.relation.issn","0021-9533"],["dc.title","sigma 1B adaptin regulates adipogenesis by mediating the sorting of sortilin in adipose tissue"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","752"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Traffic"],["dc.bibliographiccitation.lastpage","761"],["dc.bibliographiccitation.volume","3"],["dc.contributor.author","Reusch, Uwe"],["dc.contributor.author","Bernhard, Olaf"],["dc.contributor.author","Koszinowski, Ulrich"],["dc.contributor.author","Schu, Peter"],["dc.date.accessioned","2018-11-07T10:02:16Z"],["dc.date.available","2018-11-07T10:02:16Z"],["dc.date.issued","2002"],["dc.description.abstract","Heterotetrameric adaptor-protein complexes AP-1A and AP-3A mediate protein sorting in post-Golgi vesicular transport. AP-1A and AP-3A have been localized to the trans -Golgi network, indicating a function in protein sorting at this compartment. AP-3A appears to mediate trans -Golgi network-to-lysosome and also endosome-to-lysosome protein sorting. AP-1A is thought to be required for both trans -Golgi network-to-endosome transport and endosome-to-trans -Golgi network transport. However, the recent discovery of a role for monomeric GGA (Golgi localized gamma-ear containing, ARF binding protein) adaptor proteins in trans -Golgi network to endosome protein transport has brought into question the long-discussed trans -Golgi network-to-endosome sorting function of AP-1A. Murine cytomegalovirus gp48 contains an unusual di-leucine-based lysosome sorting signal motif and mediates lysosomal sorting of gp48/major histocompatibility complex class I receptor complexes, preventing exposure of major histocompatibility complex class I at the plasma membrane. We analyzed lysosomal sorting of gp48/major histocompatibility complex class I receptor complexes in cell lines deficient for AP-1A, AP-3A and both, to determine their sorting functions. We find that AP1-A and AP3-A mediate distinct and sequential steps in the lysosomal sorting. Both sorting functions are required to prevent MHC class I exposure at the plasma membrane at steady-state."],["dc.identifier.doi","10.1034/j.1600-0854.2002.31007.x"],["dc.identifier.isi","000178003100007"],["dc.identifier.pmid","12230473"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38189"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.notes.submitter","Najko"],["dc.relation.issn","1398-9219"],["dc.title","AP-1A and AP-3A lysosomal sorting functions"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2385"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Molecular Biology of the Cell"],["dc.bibliographiccitation.lastpage","2398"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Lui, WWY"],["dc.contributor.author","Collins, B. M."],["dc.contributor.author","Hirst, J."],["dc.contributor.author","Motley, A."],["dc.contributor.author","Millar, Catherine B."],["dc.contributor.author","Schu, Peter Valentin"],["dc.contributor.author","Owen, D. J."],["dc.contributor.author","Robinson, M. S."],["dc.date.accessioned","2018-11-07T10:38:43Z"],["dc.date.available","2018-11-07T10:38:43Z"],["dc.date.issued","2003"],["dc.description.abstract","The adaptor appendage domains are believed to act as binding platforms for coated vesicle accessory proteins. Using glutathione S-transferase pulldowns from pig brain cytosol, we find three proteins that can bind to the appendage domains of both the AP-1 gamma subunit and the GGAs: gamma-synergin and two novel proteins, p56 and p200. p56 elicited better antibodies than p200 and was generally more tractable. Although p56 and gamma-synergin bind to both GGA and gamma appendages in vitro, immunofluorescence labeling of nocodazole-treated cells shows that p56 colocalizes with GGAs on TGN46-positive membranes, whereas gamma-synergin colocalizes with AP-1 primarily on a different membrane compartment. Furthermore, in AP-1-deficient cells, p56 remains membrane-associated whereas gamma-synergin becomes cytosolic. Thus, p56 and gamma-synergin show very strong preferences for GGAs and AP-1, respectively, in vivo. However, the GGA and gamma appendages share the same fold as determined by x-ray crystallography, and mutagenesis reveals that the same amino acids contribute to their binding sites. By overexpressing wild-type GGA and gamma appendage domains in cells, we can drive p56 and gamma-synergin, respectively, into the cytosol, suggesting a possible mechanism for selectively disrupting the two pathways."],["dc.identifier.doi","10.1091/mbc.E02-11-0735"],["dc.identifier.isi","000183524100017"],["dc.identifier.pmid","12808037"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/45878"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Cell Biology"],["dc.relation.issn","1059-1524"],["dc.title","Binding partners for the COOH-Terminal appendage domains of the GGAs and gamma-adaptin"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","525"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Developmental Cell"],["dc.bibliographiccitation.lastpage","538"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Saint-Pol, A."],["dc.contributor.author","Yelamos, B."],["dc.contributor.author","Amessou, M."],["dc.contributor.author","Mills, I. G."],["dc.contributor.author","Dugast, M."],["dc.contributor.author","Tenza, D."],["dc.contributor.author","Schu, Peter Valentin"],["dc.contributor.author","Antony, C."],["dc.contributor.author","McMahon, Harvey T."],["dc.contributor.author","Lamaze, C."],["dc.contributor.author","Johannes, L."],["dc.date.accessioned","2018-11-07T10:49:49Z"],["dc.date.available","2018-11-07T10:49:49Z"],["dc.date.issued","2004"],["dc.description.abstract","Retrograde transport links early/recycling endosomes to the trans-Golgi network (TGN), thereby connecting the endocytic and the biosynthetic/secretory pathways. To determine how internalized molecules are targeted to the retrograde route, we have interfered with the function of clathrin and that of two proteins that interact with it, AP1 and epsinR. We found that the glycosphingolipid binding bacterial Shiga toxin entered cells efficiently when clathrin expression was inhibited. However, retrograde transport of Shiga toxin to the TGN was strongly inhibited. This allowed us to show that for Shiga toxin, retrograde sorting on early/ recycling endosomes depends on clathrin and epsinR, but not AP1. EpsinR was also involved in retrograde transport of two endogenous proteins, TGN38/46 and mannose 6-phosphate receptor. In conclusion, our work reveals the existence of clathrin-independent and -dependent transport steps in the retrograde route, and establishes a function for clathrin and epsinR at the endosome-TGN interface."],["dc.identifier.doi","10.1016/S1534-5807(04)00100-5"],["dc.identifier.isi","000222443000011"],["dc.identifier.pmid","15068792"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/48517"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.relation.issn","1534-5807"],["dc.title","Clathrin adaptor epsinR is required for retrograde sorting on early endosomal membranes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","121"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Traffic"],["dc.bibliographiccitation.lastpage","132"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Medigeshi, Guruprasad R."],["dc.contributor.author","Krikunova, Maria"],["dc.contributor.author","Radhakrishnan, Karthikeyan"],["dc.contributor.author","Wenzel, Dirk"],["dc.contributor.author","Klingauf, Juergen"],["dc.contributor.author","Schu, Peter"],["dc.date.accessioned","2018-11-07T11:20:52Z"],["dc.date.available","2018-11-07T11:20:52Z"],["dc.date.issued","2008"],["dc.description.abstract","The adaptor protein complex AP-1 mediates vesicular protein sorting between the trans Golgi network and endosomes. AP-1 recycles between membranes and the cytoplasm together with clathrin during transport vesicle formation and vesicle uncoating. AP-1 recycles independent of clathrin, indicating binding to unproductive membrane domains and premature termination of vesicle budding. Membrane recruitment requires ADP ribosylation factor-1-GTP, a transmembrane protein containing an AP-1-binding motif and phosphatidyl-inositol phosphate (PI-4-P). Little is known about the regulation of AP-1 membrane-cytoplasm recycling. We identified the N-terminal domain of mu 1A-adaptin as being involved in the regulation of AP-1 membrane-cytoplasm recycling by constructing chimeras of mu 1A and its homologue mu 2. The AP-1 complex containing this mu 2-mu 1A chimera had slowed down recycling kinetics, resulting in missorting of mannose 6-phosphate receptors. The N-terminal domain is only accessible from the cytoplasmic AP-1 surface. None of the proteins known to influence AP-1 membrane recycling bound to this mu 1A domain, indicating the regulation of AP-1 membrane-cytoplasm recycling by an yet unidentified cytoplasmic protein."],["dc.identifier.doi","10.1111/j.1600-0854.2007.00672.x"],["dc.identifier.isi","000251588300011"],["dc.identifier.pmid","17988225"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/55638"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Blackwell Publishing"],["dc.relation.issn","1398-9219"],["dc.title","AP-1 membrane-cytoplasm recycling regulated by mu 1A-adaptin"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","595"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","The Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","606"],["dc.bibliographiccitation.volume","152"],["dc.contributor.author","Folsch, H."],["dc.contributor.author","Pypaert, M."],["dc.contributor.author","Schu, Peter Valentin"],["dc.contributor.author","Mellman, I."],["dc.date.accessioned","2018-11-07T09:22:22Z"],["dc.date.available","2018-11-07T09:22:22Z"],["dc.date.issued","2001"],["dc.description.abstract","Expression of the epithelial cell-specific heterotetrameric adaptor complex AP-1B is required for the polarized distribution of man!: membrane proteins to the basolateral surface of LLC-PK1 kidney cells. AP-1B is distinguished from the ubiquitously expressed AP-1A by exchange of its single 50-kD mu subunit, mu 1A, being replaced by the closely related mu 1B. Here we show that this substitution is sufficient to couple basolateral plasma membrane proteins, such as a low-density lipoprotein receptor (LDLR), to the AP-1B complex and to clathrin. The interaction between LDLR and AP-1B is likely to occur in the trans-Golgi network (TGN), as was suggested by the localization of functional, epitope-tagged mu1 by immunofluorescence and immunoelectron microscopy. Tagged AP-1A and AP 1B complexes were found in the perinuclear region close to the Golgi complex and recycling endosomes, often in clathrin-coated buds and vesicles. Yet, AP-1A and AP-1B localized to different subdomains of the TGN, with only AP-1A colocalizing with furin, a membrane protein that uses AP-1 to recycle between the TGN and endosomes. We conclude that AP-1B functions by interacting with its cargo molecules and clathrin in the TGN, where it acts to sort basolateral proteins from proteins destined for the apical surface and from those selected by AP-1A for transport to endosomes and lysosomes."],["dc.description.sponsorship","NIGMS NIH HHS [GM29765, R01 GM029765]"],["dc.identifier.doi","10.1083/jcb.152.3.595"],["dc.identifier.isi","000166882900014"],["dc.identifier.pmid","11157985"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/29327"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Rockefeller Univ Press"],["dc.relation.issn","0021-9525"],["dc.title","Distribution and function of AP-1 clathrin adaptor complexes in polarized epithelial cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]