Plakoglobin
Plakoglobin, also known as junction plakoglobin or gamma-catenin, is a
arrhythmogenic right ventricular dysplasia
.
Structure
Human plakoglobin is 81.7 kDa in molecular weight and 745 amino acids long.E-cadherin; in that context, it was called gamma-catenin. Plakoglobin forms distinct complexes with cadherins and desmosomal cadherins.
Function
Plakoglobin is a major
Plakoglobin is essential for normal development of
cardiac fibers obtained from JUP-null embryonic mice had decreased passive compliance albeit normal attachment of sarcomeres to adherens junctions.[14]
In additional studies, an inducible
Intracellular plakoglobin expression is controlled by
glycogen synthase kinase 3β (GSK3β) and scaffold proteins adenomatous polyposis coli (APC) and axin targets plakoglobin for degradation.[18][19][20][31–33]. The phosphorylated motif is recognized by β-TrCP, a ubiquitin ligase that targets plakoglobin 26S proteasome-dependent degradation.[21] Plakoglobin is also O-glycosylated near its N-terminal
destruction box.
Clinical significance
Mutation of the JUP gene encoding plakoglobin has been implicated as one of the causes of the
ARVD
by early adolescence.
It has become clear that
ARVC is a disease of the cardiac muscle desmosome; advances in molecular genetics have illuminated this notion.[28][29][30][31][32][33][34][35][36]
Studies investigating the role of plakoglobin in disease pathology have found that suppression of
siRNA led to the nuclear localization of plakoglobin, resulting in a reduction in Wnt signaling via Tcf/Lef1 and ensued pathogenesis of ARVC.[37] Specifically, adipogenic factor expression was induced and cardiac progenitor cells at the epicardium were differentiated to adipocytes.[38]
Non-invasive
ARVC.[40]
Abnormal distribution of plakoglobin due to mutations in genes encoding for Desmoglein 1 and 3 have also been implicated in Pemphigus vulgaris.[41][42]
Interactions
Plakoglobin has been shown to
interact
with:
See also
- Catenin
- List of conditions caused by problems with junctional proteins
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000173801 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000001552 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ a b "Entrez Gene: JUP junction plakoglobin".
- ^ "Protein sequence of human JUP (Uniprot ID: P14923)". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB). Archived from the original on 24 September 2015. Retrieved 3 July 2015.
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Further reading
- Cowin P, Kapprell HP, Franke WW, Tamkun J, Hynes RO (Sep 1986). "Plakoglobin: a protein common to different kinds of intercellular adhering junctions". Cell. 46 (7): 1063–73. S2CID 45332970.
- Franke WW, Goldschmidt MD, Zimbelmann R, Mueller HM, Schiller DL, Cowin P (Jun 1989). "Molecular cloning and amino acid sequence of human plakoglobin, the common junctional plaque protein". Proceedings of the National Academy of Sciences of the United States of America. 86 (11): 4027–31. PMID 2726765.
- Mathur M, Goodwin L, Cowin P (May 1994). "Interactions of the cytoplasmic domain of the desmosomal cadherin Dsg1 with plakoglobin". The Journal of Biological Chemistry. 269 (19): 14075–80. PMID 8188687.
- Beavon IR (Aug 2000). "The E-cadherin-catenin complex in tumour metastasis: structure, function and regulation". European Journal of Cancer. 36 (13 Spec No): 1607–20. PMID 10959047.
- Wilson PD (Apr 2001). "Polycystin: new aspects of structure, function, and regulation". Journal of the American Society of Nephrology. 12 (4): 834–45. PMID 11274246.
- Protonotarios NI, Tsatsopoulou AA, Gatzoulis KA (Feb 2002). "Arrhythmogenic right ventricular cardiomyopathy caused by a deletion in plakoglobin (Naxos disease)". Cardiac Electrophysiology Review. 6 (1–2): 72–80. PMID 11984022.
- Knudsen KA, Wheelock MJ (Aug 1992). "Plakoglobin, or an 83-kD homologue distinct from beta-catenin, interacts with E-cadherin and N-cadherin". The Journal of Cell Biology. 118 (3): 671–9. PMID 1639850.
- Arnemann J, Spurr NK, Wheeler GN, Parker AE, Buxton RS (Jul 1991). "Chromosomal assignment of the human genes coding for the major proteins of the desmosome junction, desmoglein DGI (DSG), desmocollins DGII/III (DSC), desmoplakins DPI/II (DSP), and plakoglobin DPIII (JUP)". Genomics. 10 (3): 640–5. PMID 1889810.
- Kinch MS, Clark GJ, Der CJ, Burridge K (Jul 1995). "Tyrosine phosphorylation regulates the adhesions of ras-transformed breast epithelia". The Journal of Cell Biology. 130 (2): 461–71. PMID 7542250.
- Aberle H, Bierkamp C, Torchard D, Serova O, Wagner T, Natt E, Wirsching J, Heidkämper C, Montagna M, Lynch HT (Jul 1995). "The human plakoglobin gene localizes on chromosome 17q21 and is subjected to loss of heterozygosity in breast and ovarian cancers". Proceedings of the National Academy of Sciences of the United States of America. 92 (14): 6384–8. PMID 7604000.
- Sacco PA, McGranahan TM, Wheelock MJ, Johnson KR (Aug 1995). "Identification of plakoglobin domains required for association with N-cadherin and alpha-catenin". The Journal of Biological Chemistry. 270 (34): 20201–6. PMID 7650039.
- Daniel JM, Reynolds AB (Sep 1995). "The tyrosine kinase substrate p120cas binds directly to E-cadherin but not to the adenomatous polyposis coli protein or alpha-catenin". Molecular and Cellular Biology. 15 (9): 4819–24. PMID 7651399.
- Kanai Y, Ochiai A, Shibata T, Oyama T, Ushijima S, Akimoto S, Hirohashi S (Mar 1995). "c-erbB-2 gene product directly associates with beta-catenin and plakoglobin". Biochemical and Biophysical Research Communications. 208 (3): 1067–72. PMID 7702605.
- Roh JY, Stanley JR (May 1995). "Plakoglobin binding by human Dsg3 (pemphigus vulgaris antigen) in keratinocytes requires the cadherin-like intracytoplasmic segment". The Journal of Investigative Dermatology. 104 (5): 720–4. PMID 7738346.
- Shibamoto S, Hayakawa M, Takeuchi K, Hori T, Miyazawa K, Kitamura N, Johnson KR, Wheelock MJ, Matsuyoshi N, Takeichi M (Mar 1995). "Association of p120, a tyrosine kinase substrate, with E-cadherin/catenin complexes". The Journal of Cell Biology. 128 (5): 949–57. PMID 7876318.
- Rubinfeld B, Souza B, Albert I, Munemitsu S, Polakis P (Mar 1995). "The APC protein and E-cadherin form similar but independent complexes with alpha-catenin, beta-catenin, and plakoglobin". The Journal of Biological Chemistry. 270 (10): 5549–55. PMID 7890674.
- Troyanovsky SM, Troyanovsky RB, Eshkind LG, Leube RE, Franke WW (Nov 1994). "Identification of amino acid sequence motifs in desmocollin, a desmosomal glycoprotein, that are required for plakoglobin binding and plaque formation". Proceedings of the National Academy of Sciences of the United States of America. 91 (23): 10790–4. PMID 7971964.
- Shibata T, Gotoh M, Ochiai A, Hirohashi S (Aug 1994). "Association of plakoglobin with APC, a tumor suppressor gene product, and its regulation by tyrosine phosphorylation". Biochemical and Biophysical Research Communications. 203 (1): 519–22. PMID 8074697.
- Hinck L, Näthke IS, Papkoff J, Nelson WJ (Jun 1994). "Dynamics of cadherin/catenin complex formation: novel protein interactions and pathways of complex assembly". The Journal of Cell Biology. 125 (6): 1327–40. PMID 8207061.
- Arnemann J, Sullivan KH, Magee AI, King IA, Buxton RS (Mar 1993). "Stratification-related expression of isoforms of the desmosomal cadherins in human epidermis". Journal of Cell Science. 104 (3): 741–50. PMID 8314871.
- Ozawa M, Nuruki K, Toyoyama H, Ohi Y (Oct 1995). "Cloning of an alternative form of plakoglobin (gamma-catenin) lacking the fourth armadillo repeat". Journal of Biochemistry. 118 (4): 836–40. PMID 8576101.
- Fuchs M, Müller T, Lerch MM, Ullrich A (Jul 1996). "Association of human protein-tyrosine phosphatase kappa with members of the armadillo family". The Journal of Biological Chemistry. 271 (28): 16712–9. PMID 8663237.