The Epithelia-Specific Membrane Trafficking Factor AP-1B Controls Gut Immune Homeostasis in Mice

Takahashi, Daisuke; Hase, Koji; Kimura, Shunsuke; Nakatsu, Fubito; Ohmae, Masumi; Mandai, Yasushi; Satô, Tôru; Date, Yasuhiro; Ebisawa, Masashi; Kato, Tamotsu; Obata, Yuichi; Fukuda, Shinji; Kawamura, Yuki I.; Dohi, Taeko; Katsuno, Tatsuro; Yokosuka, Osamu; Waguri, Satoshi; Ohno, Hiroshi

doi:10.1053/j.gastro.2011.04.056

Cited by 53 publications

(60 citation statements)

References 33 publications

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“…That both AP-1A and AP-1B play key roles in basolateral trafficking highlight the importance of AP-1 as a master regulator of epithelial polarity, consistent with other findings implicating AP-1 in neuronal polarity (35) and as a key requirement in early development of multicellular organisms (36,37). Recent observations indicating that AP-1B levels may be decreased in some forms of Crohn disease and that mice knockout for AP-1B develop colon inflamation (34), suggest that investigating changes in polarity of CAR may provide new avenues for translational research in intestinal disease.…”

Section: Discussionsupporting

confidence: 85%

“…For example, it has been shown that several epithelia do not express AP-1B-for example, liver (12,32), retinal pigment epithelium (6), and kidney proximal tubule (33)-and that knockout of μ1B in mice is not lethal (34). That both AP-1A and AP-1B play key roles in basolateral trafficking highlight the importance of AP-1 as a master regulator of epithelial polarity, consistent with other findings implicating AP-1 in neuronal polarity (35) and as a key requirement in early development of multicellular organisms (36,37).…”

Section: Discussionmentioning

confidence: 99%

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Basolateral sorting of the coxsackie and adenovirus receptor through interaction of a canonical YXXΦ motif with the clathrin adaptors AP-1A and AP-1B

Carvajal-González

Gravotta

Mattera

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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The coxsackie and adenovirus receptor (CAR) plays key roles in epithelial barrier function at the tight junction, a localization guided in part by a tyrosine-based basolateral sorting signal, 318 YNQV 321 . Sorting motifs of this type are known to route surface receptors into clathrin-mediated endocytosis through interaction with the medium subunit (μ2) of the clathrin adaptor AP-2, but how they guide new and recycling membrane proteins basolaterally is unknown. Here, we show that YNQV functions as a canonical YxxΦ motif, with both Y318 and V321 required for the correct basolateral localization and biosynthetic sorting of CAR, and for interaction with a highly conserved pocket in the medium subunits (μ1A and μ1B) of the clathrin adaptors AP-1A and AP-1B. Knock-down experiments demonstrate that AP-1A plays a role in the biosynthetic sorting of CAR, complementary to the role of AP-1B in basolateral recycling of this receptor. Our study illustrates how two clathrin adaptors direct basolateral trafficking of a plasma membrane protein through interaction with a canonical YxxΦ motif.trans-Golgi network | recycling endosomes | exocytosis | epithelial cells | protein sorting

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Section: Discussionsupporting

confidence: 85%

Section: Discussionmentioning

confidence: 99%

Basolateral sorting of the coxsackie and adenovirus receptor through interaction of a canonical YXXΦ motif with the clathrin adaptors AP-1A and AP-1B

Carvajal-González

Gravotta

Mattera

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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“…Our knowledge about the functions of these complexes and the underlying molecular mechanisms is very limited. Although knockouts of the ubiquitously expressed isoforms are embryonic lethal, knockouts of tissue-specific isoforms are viable, but reveal impaired tissue functions (Glyvuk et al, 2010;Meyer et al, 2000;Takahashi et al, 2011;Zizioli et al, 2010;Zizioli et al, 1999). s1A is ubiquitously expressed at comparable levels in most tissues, whereas its expression in brain is several-fold higher.…”

Section: Discussionmentioning

confidence: 99%

σ1B-adaptin sorts sortilin in adipose tissue regulating adipogenesis

Baltes

Larsen

Radhakrishnan

et al. 2014

Journal of Cell Science

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BSTRACTHere, we describe altered sorting of sortilin in adipocytes deficient for the s1B-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 s1 subunit isoforms -s1A, s1B and s1C (also known as AP1S1, AP1S2 and AP1S3, respectively). s1B-deficient mice display impaired recycling of synaptic vesicles and lipodystrophy. Here, we show that sortilin is overexpressed in adipose tissue from s1B 2/2 mice, and that its overexpression in wild-type cells is sufficient to suppress adipogenesis. s1B-specific binding of sortilin requires the sortilin DxxD-x12-DSxxxL motif. s1B 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 s1B 2/2 mice, although this is the tissue with the highest expression of s1B and sortilin. Thus, adipose-tissue-specific and s1B-dependent routes for the transport of sortilin exist and are involved in the regulation of adipogenesis and adipose-tissue mass.

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“…23 Importantly, histological studies suggested that more than 80% of kidney cancers arise from the proximal kidney tubules, [82][83][84] and AP-1B expression is down regulated in mouse models for colon cancer. 85 Furthermore, AP-1B was also found to be reduced in the colon of Crohn's disease patients, 86 and m1B knock out mice suffer from proliferation defects and hyperplasia in their intestine. 87 These observations highlight the importance of AP-1B in epithelial cell maintenance.…”

Section: Expression Pattern Of Ap-1bmentioning

confidence: 99%

Role of the epithelial cell-specific clathrin adaptor complex AP-1B in cell polarity

Fölsch¹

2015

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The Epithelia-Specific Membrane Trafficking Factor AP-1B Controls Gut Immune Homeostasis in Mice

Cited by 53 publications

References 33 publications

Basolateral sorting of the coxsackie and adenovirus receptor through interaction of a canonical YXXΦ motif with the clathrin adaptors AP-1A and AP-1B

Basolateral sorting of the coxsackie and adenovirus receptor through interaction of a canonical YXXΦ motif with the clathrin adaptors AP-1A and AP-1B

σ1B-adaptin sorts sortilin in adipose tissue regulating adipogenesis

Role of the epithelial cell-specific clathrin adaptor complex AP-1B in cell polarity

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