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000128277 0247_ $$2doi$$a10.1007/s12013-013-9811-5
000128277 0247_ $$2pmid$$apmid:24399133
000128277 0247_ $$2ISSN$$a0163-4992
000128277 0247_ $$2ISSN$$a1085-9195
000128277 0247_ $$2ISSN$$a1559-0283
000128277 037__ $$aDKFZ-2017-04294
000128277 041__ $$aeng
000128277 082__ $$a570
000128277 1001_ $$0P:(DE-HGF)0$$aSchmitt, Melanie$$b0$$eFirst author
000128277 245__ $$aMutation of human connexin43 amino acids s279/s282 increases protein stability upon treatment with epidermal growth factor.
000128277 260__ $$aNew York, NY$$bSpringer$$c2014
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000128277 520__ $$aConnexins are the structural units of gap junctions, structures allowing interchanging of information between the adjacent cells. Connexin43 (Cx43) is the most abundant gap junction protein. Cx43 can be degraded by lysosome- and proteasome-mediated processes upon internalisation of the entire structure. Only little is known about the role of phosphorylation during the gap junction degradation. In Cx43, a protein containing 14 amino acids susceptible to be phosphorylated, amino acids S279 and S282 are phosphorylated upon epidermal growth factor (EGF) treatment by erk1/2 MAP kinases. Here, we show that the wild-type Cx43 protein, as well as HeLa cells expressing the mutated Cx43 proteins S279A, S282A, and S279A/S282A, is mainly located at the plasma membrane. However, the protein stability is not altered in the isolated single mutants, whereas the double mutant S279A/S282A is strongly degradation impaired upon EGF treatment. This effect is not due to the decreased Cx43 internalisation, but seems to be related to a reduced ubiquitination.
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000128277 650_7 $$2NLM Chemicals$$aConnexin 43
000128277 650_7 $$062229-50-9$$2NLM Chemicals$$aEpidermal Growth Factor
000128277 650_7 $$0EC 2.7.11.24$$2NLM Chemicals$$aMitogen-Activated Protein Kinase 1
000128277 650_7 $$0EC 2.7.11.24$$2NLM Chemicals$$aMitogen-Activated Protein Kinase 3
000128277 7001_ $$0P:(DE-HGF)0$$aLeykauf, Kerstin$$b1
000128277 7001_ $$0P:(DE-He78)79ee80b202aec5884065e0d894481c95$$aReinz, Eileen$$b2$$udkfz
000128277 7001_ $$0P:(DE-HGF)0$$aCheng, Hao$$b3
000128277 7001_ $$0P:(DE-He78)0e9c7f8ab141d513965e8f2237a716b7$$aAlonso, Angel$$b4$$udkfz
000128277 7001_ $$0P:(DE-He78)1b0532fc51fd835d3bb64196e6e751fc$$aSchenkel, Johannes$$b5$$eLast author$$udkfz
000128277 773__ $$0PERI:(DE-600)2072590-5$$a10.1007/s12013-013-9811-5$$gVol. 69, no. 2, p. 379 - 384$$n2$$p379 - 384$$tCell biochemistry and biophysics$$v69$$x1559-0283$$y2014
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000128277 9141_ $$y2014
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