Kegg Pathway: Adherens junction

KEGG ID: 04520

Reference Diagram

KEGG Diagram for Adherens junction

Rat

There are 70 IPI Records from this pathway found in Rattus norvegicus.

Location of Adherens junction proteins on Rat Genome

IPI Record Position
1: Acp1 6:48782802-48798831
2: Actb 12:12047070-12050051
3: Actg1 10:109773489-109777655
4: Actn1 6:103110009-103282917
5: Actn2_predicted 17:68670924-68773261
6: Actn3 1:207475569-207492267
7: Actn4 1:84000723-84073767
8: Acvr1b 7:139937993-139958724
9: Acvr1c 3:40027228-40102299
10: Af6 1:48827689-48911351
11: Baiap2 10:109351262-109418859
12: Catna1 18:27629915-27769375
13: Cdc42 5:156106131-156143040
14: Cdh1 19:36442693-36512091
15: Crebbp 10:11598680-11724122
16: Csnk2a1 3:142588572-142609301
17: Csnk2a2_predicted 19:10015349-10049896
18: Csnk2b 20:3764565-3768982
19: Ctnna2_predicted 4:110776309-111694975
20: Ctnnb1 8:125978161-125987670
21: Ctnnd1_predicted 3:67809064-67860234
22: Egfr 14:97617358-97788213
23: Erbb2 10:87219085-87242919
24: Farp2_predicted 9:92807930-92907102
25: Fgfr1 16:70869944-70924029
26: Fyn 20:43501853-43695567
27: Igf1r 1:122704987-122989472
28: Insr 12:2957511-3086795
29: IPI00765011 :-
30: IPI00766566 :-
31: Iqgap1_predicted 1:136553443-136644285
32: Lef1 2:228550263-228689323
33: LMO7 15:85792940-85928469
34: Map3k7_predicted 5:48252637-48308832
35: Mapk1 11:85968732-86030389
36: Mapk3 1:185935044-185941249
37: Met 4:43134183-43211357
38: Pard3 19:57016001-57601905
39: Ptpn1 3:159070431-159119162
40: Ptpn6 4:160843701-160856821
41: Ptprb_predicted 7:55615163-55711352
42: Ptprj 3:74796435-74935394
43: Ptprm 9:105785707-106503104
44: Pvrl1 8:46739494-46798633
45: Pvrl2 1:79021827-79059686
46: Pvrl3_predicted 11:55843791-55940545
47: Rac1 12:11380314-11400531
48: Rac2 7:116520066-116532482
49: RGD1559455_predicted 20:24686070-25040014
50: RGD1559826_predicted 13:87276201-87293415
51: RGD1561602_predicted 10:64681467-64804864
52: RGD1562230_predicted 20:25900952-26268772
53: Rhoa :-
54: Smad2 18:73180290-73241713
55: Smad3 8:67803909-67952056
56: Smad4 18:70432832-70461485
57: Snai1 3:158676980-158681471
58: Snai2 :-
59: Src 3:148157256-148170524
60: Ssx2ip 2:244604360-244638522
61: Tcf3_predicted 4:106128505-106149235
62: Tcf7_predicted 10:37687192-37716600
63: Tgfbr1 5:63976868-64034058
64: Tgfbr2 8:120593595-120680453
65: Tjp1_predicted 1:119686175-119750533
66: Vcl_predicted 15:3480195-3654131
67: Wasf1 :-
68: Wasf2 5:151930684-151948306
69: Was_predicted X:26434165-26444819
70: Yes1 9:112516842-112563988

Mouse

There are 70 IPI Records from this pathway found in Mus musculus.

Location of Adherens junction proteins on Mouse Genome

IPI Record Position
1: Acp1 12:31479708-31497634
2: Actb 5:143168256-143171864
3: Actg1 11:120161781-120164582
4: Actn1 12:81086385-81179156
5: Actn2 13:12323759-12395065
6: Actn3 19:4861223-4877884
7: Actn4 7:28602011-28671040
8: Acvr1b 15:101002159-101040635
9: Acvr1c 2:58087208-58140193
10: Baiap2 11:119758853-119822869
11: Cdc42 4:136591778-136629755
12: Cdh1 8:109492497-109559375
13: Crebbp 16:3999276-4128632
14: Csnk2a1 2:151918326-151973281
15: Csnk2a2 8:98337108-98377956
16: Csnk2b 17:34724251-34729503
17: Ctnna1 18:35244863-35380747
18: Ctnna2 6:76812059-77775094
19: Ctnna3 10:62899394-64398190
20: Ctnnb1 9:120782173-120809205
21: Ctnnd1 2:84401622-84451514
22: Egfr 11:16652206-16813912
23: Erbb2 11:98228574-98253806
24: Farp2 1:95358974-95452378
25: Fert2 17:63581484-63824640
26: Fgfr1 8:26997826-27039466
27: Fyn 10:39059219-39254797
28: Igf1r 7:67826372-68100293
29: Insr 8:3155401-3279128
30: Iqgap1 7:80586294-80676807
31: Lef1 3:131099626-131213476
32: Lmo7 14:100725118-100821293
33: Map3k7 4:32292729-32349408
34: Mapk1 16:16896945-16961016
35: Mapk3 7:126550780-126556964
36: Met 6:17441241-17521823
37: Nlk 11:78383361-78513568
38: Pard3 8:129950335-130496920
39: Ptpn1 2:167623614-167668115
40: Ptpn6 6:124686727-124698484
41: Ptprb 10:115679633-115785122
42: Ptprf 4:117707733-117775378
43: Ptprj 2:90233731-90381407
44: Ptprm 17:66571893-67259402
45: Pvrl1 9:43495571-43558456
46: Pvrl2 7:18875186-18908047
47: Pvrl3 16:46314342-46416301
48: Pvrl4 1:173207030-173225256
49: Rac1 5:143761100-143783654
50: Rac2 15:78386424-78400038
51: Rac3 11:120537558-120540059
52: Rhoa 9:108164298-108196026
53: Smad2 18:76367274-76431096
54: Smad3 9:63444773-63556000
55: Smad4 :-
56: Snai1 2:167229432-167234019
57: Snai2 16:14619437-14622963
58: Sorbs1 19:40348360-40451928
59: Src 2:157115730-157163279
60: Ssx2ip 3:146342041-146377521
61: Tcf3 6:72555889-72718465
62: Tcf7 11:52096027-52126602
63: Tcf7l2 19:55795070-55986503
64: Tgfbr1 4:47374405-47436024
65: Tgfbr2 9:115932995-116023987
66: Tjp1 7:65175115-65250189
67: Vcl 14:19717950-19822228
68: Was X:7238425-7247411
69: Wasf1 10:40571988-40626982
70: Wasf2 4:132402654-132471805
71: Wasf3 5:146689240-146774650
72: Wasl 6:24563813-24614998
73: Yes1 5:32887814-32963638

Human

There are 70 IPI Records from this pathway found in Homo sapiens.

Location of Adherens junction proteins on Human Genome

IPI Record Position
1: ACP1 2:254869-268283
2: ACTB 7:5533313-5535814
3: ACTN1 14:68410793-68515747
4: ACTN2 1:234916431-234994554
5: ACTN3 11:66070967-66087373
6: ACTN4 19:43830167-43913010
7: ACVR1B 12:50494095-50677124
8: ACVR1C 2:158097152-158193645
9: BAIAP2 17:76623557-76705827
10: CDC42 1:22235157-22292024
11: CDH1 16:67328696-67426943
12: CREBBP 16:3716572-3870723
13: CSNK2A1 20:411340-472482
14: CSNK2A2 16:56749320-56789283
15: CTNNA1 5:138117006-138298619
16: CTNNA2 2:79732191-80729415
17: CTNNA3 10:67349725-69125933
18: CTNNB1 3:41216004-41256938
19: CTNND1 11:57236618-57343226
20: EGFR 7:55054219-55242524
21: EP300 22:39817736-39905472
22: ERBB2 17:35104766-35138441
23: FARP2 2:241944384-242082928
24: FER 5:108111422-108560441
25: FGFR1 8:38389406-38445296
26: FYN 6:112088228-112301348
27: IGF1R 15:97010302-97319034
28: INSR 19:7067049-7245045
29: IQGAP1 15:88732477-88846479
30: LEF1 4:109188150-109309027
31: LMO7 13:75092571-75343063
32: MAP3K7 6:91280013-91353485
33: MAPK1 22:20446873-20551730
34: MAPK3 16:30032951-30042116
35: MET 7:116099695-116223632
36: MLLT4 6:167970520-168115552
37: NLK 17:23393309-23547529
38: PARD3 10:34438495-35144255
39: PTPN1 20:48560294-48634706
40: PTPN6 12:6930763-6940740
41: PTPRB 12:69201231-69317469
42: PTPRF 1:43769134-43861924
43: PTPRJ 11:47958689-48146246
44: PTPRM 18:7557817-8396160
45: PVRL1 11:119014018-119104645
46: PVRL2 19:50041390-50083476
47: PVRL3 3:112273555-112395063
48: PVRL4 1:159307409-159326013
49: RAC1 7:6380651-6410120
50: RAC2 22:35951238-35970241
51: RAC3 17:77582821-77585366
52: RHOA 3:49371585-49424530
53: SMAD2 18:43618435-43711221
54: SMAD3 15:65145249-65274586
55: SMAD4 18:46810611-46860142
56: SNAI1 20:48032934-48038825
57: SNAI2 8:49992802-49996541
58: SORBS1 10:97061520-97311161
59: SRC 20:35406502-35467239
60: SSX2IP 1:84881978-84928816
61: TCF7 5:133478301-133511826
62: TCF7L1 2:85214245-85391012
63: TCF7L2 10:114700201-114917427
64: TGFBR1 9:100907233-100956406
65: TGFBR2 3:30622998-30710635
66: TJP1 15:27779656-27902010
67: VCL 10:75427878-75549924
68: WAS X:48427112-48434762
69: WASF1 6:110528382-110607819
70: WASF2 1:27603317-27689256
71: WASF3 13:26029840-26161085
72: WASL 7:123109237-123176352
73: YES1 18:711747-802547

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Recent Literature

Modulation of intracellular trafficking regulates cell intercalation in the Drosophila trachea.

Nat Cell Biol. 2008 Jul 20;
Shaye DD, Casanova J, Llimargas M

Through intercalation, a fundamental mechanism underlying elongation during morphogenesis, epithelial cells exchange places in a spatially oriented manner. Epithelial cells are tightly coupled through distinct intercellular junctions, including Adherens junctions. Whether trafficking-mediated regulation of adhesion through Adherens junctions modulates intercalation in vivo remains controversial. In Drosophila melanogaster, cells in most branches intercalate during tracheal development. However, Wingless (Wg)-promoted expression of the transcription factor Spalt (Sal) in the dorsal trunk inhibits intercalation by an unknown mechanism. Here we have examined the role of trafficking in tracheal intercalation and show that it requires endocytosis, whereas it is opposed by Rab11-mediated recycling in the dorsal trunk. Subapical Rab11 accumulation is enhanced by sal and elevated Rab11-mediated recycling occurs in the dorsal trunk, suggesting that upregulation of Rab11 is one way in which sal inhibits intercalation. We found that dRip11, which regulates Rab11 localization and function, is regulated by sal and can modulate intercalation. Finally, we provide evidence that levels of E-cadherin (DE-cad), an Adherens junction component and Rab11-compartment cargo, are dynamically regulated by trafficking during tracheal development, and that such regulation modulates intercalation. Our work suggests a mechanism by which trafficking of adhesion molecules regulates intercalation, and shows how this mechanism can be modulated in vivo to influence cell behaviour.

p120-catenin regulates leukocyte transmigration through an effect on VE-cadherin phosphorylation.

Blood. 2008 Jul 18;
Alcaide P, Newton G, Auerbach S, Sehrawat S, Mayadas TN, Golan DE, Yacono P, Vincent P, Kowalczyk A, Luscinskas FW

Vascular Endothelial-Cadherin (VE-cad) is localized to Adherens junctions at endothelial cell borders and forms a complex with alpha-, beta-, gamma- and p120-catenins (p120). We previously showed that the VE-cad complex disassociates to form short-lived "gaps" during leukocyte transendothelial migration (TEM)(1); however, whether these gaps are required for leukocyte TEM is not clear. Recently p120 has been shown to control VE-cad surface expression by endocytosis. We hypothesized that p120 regulates VE-cad surface expression, which would in turn have functional consequences for leukocyte transmigration. Here we show that endothelial cells transduced with an adenovirus expressing p120GFP fusion protein significantly increases VE-cad expression. Moreover, endothelial junctions with high p120GFP expression largely prevent VE-cad gap formation and neutrophil leukocyte TEM; if TEM occurs, the length of time required is prolonged. We find no evidence that VE-cad endocytosis plays a role in VE-cad gap formation and instead show that this process is regulated by changes in VE-cad phosphorylation. In fact, a non-phosphorylatable VE-cad mutant prevented TEM. In summary, our studies provide compelling evidence that VE-cad gap formation is required for leukocyte transmigration and identify p120 as a critical intracellular mediator of this process through its regulation of VE-cad expression at junctions.

The Drosophila p21 activated kinase Mbt modulates DE-cadherin mediated cell adhesion by phosphorylation of Armadillo.

Biochem J. 2008 Jul 17;
Menzel N, Melzer J, Waschke J, Lenz CE, Wecklein H, Lochnit G, Drenckhahn D, Raabe T

Phosphorylations by tyrosine and serine/threonine kinases regulate the interactions between components of the cadherin/catenin cell adhesion complex and thus can influence the dynamic modulation of cell adhesion under normal and disease conditions. Previous mutational analysis and localization experiments suggested an involvement of single members of the family of p21-activated kinases (PAKs) in the regulation of cadherin mediated cell adhesion, but the molecular mechanism remained elusive. We addressed this question using the Drosophila PAK protein Mbt, which is most similar to vertebrate PAK4. Previous phenotypic analysis showed that Mbt has a function to maintain Adherens junctions during eye development and indicated a requirement of the protein in regulation of the actin cytoskeleton and the cadherin/catenin complex. Here we show that activation of Mbt leads to destabilization of the interaction of the Drosophila beta-catenin homologue Armadillo with DE-cadherin resulting in a decrease in DE-cadherin mediated adhesion. Two conserved phosphorylation sites in Armadillo were identified that mediate this effect. Our findings support the previous observation that activation of the human Mbt homologue PAK4 leads to anchorage independent growth and provide a functional link between a PAK protein and the cadherin-catenin complex.

Jouberin localizes to collecting ducts and interacts with nephrocystin-1.

Kidney Int. 2008 Jul 16;
Eley L, Gabrielides C, Adams M, Johnson CA, Hildebrandt F, Sayer JA

Joubert syndrome and related disorders are autosomal recessive multisystem diseases characterized by cerebellar vermis aplasia/hypoplasia, retinal degeneration and cystic kidney disease. There are five known genes; mutations of which give rise to a spectrum of renal cystic diseases the most common of which is nephronophthisis, a disorder characterized by early loss of urinary concentrating ability, renal fibrosis, corticomedullary cyst formation and renal failure. Many of the proteins encoded by these genes interact with one another and are located at Adherens junctions or the primary cilia and or basal bodies. Here we characterize Jouberin, a multi-domain protein encoded by the AHI1 gene. Immunohistochemistry with a novel antibody showed that endogenous Jouberin is expressed in brain, kidney and HEK293 cells. In the kidney, Jouberin co-localized with aquaporin-2 in the collecting ducts. We show that Jouberin interacts with nephrocystin-1 as determined by yeast-2-hybrid system and this was confirmed by exogenous and endogenous co-immunoprecipitation in HEK293 cells. Jouberin is expressed at cell-cell junctions, primary cilia and basal body of mIMCD3 cells while a Jouberin-GFP construct localized to centrosomes in subconfluent and dividing MDCK cells. Our results suggest that Jouberin is a protein whose expression pattern supports both the Adherens junction and the ciliary hypotheses for abnormalities leading to nephronophthisis.Kidney International advance online publication, 16 July 2008; doi:10.1038/ki.2008.377.

Distinct molecular composition of blood and lymphatic vascular endothelial cell junctions establishes specific functional barriers within the peripheral lymph node.

Eur J Immunol. 2008 Jul 16;
Pfeiffer F, Kumar V, Butz S, Vestweber D, Imhof BA, Stein JV, Engelhardt B

Lymph nodes are strategically localized at the interfaces between the blood and lymphatic vascular system, delivering immune cells and antigens to the lymph node. As cellular junctions of endothelial cells actively regulate vascular permeability and cell traffic, we have investigated their molecular composition by performing an extensive immunofluorescence study for Adherens and tight junction molecules, including vascular endothelium (VE)-cadherin, the vascular claudins 1, 3, 5 and 12, occludin, members of the junctional adhesion molecule family plus endothelial cell-selective adhesion molecule (ESAM)-1, platelet endothelial cell adhesion molecule-1, ZO-1 and ZO-2. We found that junctions of high endothelial venules (HEV), which serve as entry site for naive lymphocytes, are unique due to their lack of the endothelial cell-specific claudin-5. LYVE-1(+) sinus-lining endothelial cells form a diffusion barrier for soluble molecules that arrive at the afferent lymph and use claudin-5 and ESAM-1 to establish characteristic tight junctions. Analysis of the spatial relationship between the different vascular compartments revealed that HEV extend beyond the paracortex into the medullary sinuses, where they are protected from direct contact with the lymph by sinus-lining endothelial cells. The specific molecular architecture of cellular junctions present in blood and lymphatic vessel endothelium in peripheral lymph nodes establishes distinct barriers controlling the distribution of antigens and immune cells within this tissue.Supporting Information for this article can be found at http//www.wiley-vch.de/contents/jc_2040/2008/38140_s.pdf.

aPKC enables development of zonula Adherens by antagonizing centripetal contraction of the circumferential actomyosin cables.

J Cell Sci. 2008 Jul 15;
Kishikawa M, Suzuki A, Ohno S

Atypical protein kinase C (aPKC) generally plays crucial roles in the establishment of cell polarity in various biological contexts. In mammalian epithelial cells, aPKC essentially works towards the transition of primordial spot-like Adherens junctions (AJs) into continuous belt-like AJs, also called zonula Adherens, lined with perijunctional actin belts. To reveal the mechanism underlying this aPKC function, we investigated the functional relationship between aPKC and myosin II, the essential role of which in epithelial-