메뉴 건너뛰기




Volumn 290, Issue 4, 2015, Pages 1952-1965

Cyclic GMP kinase II (cGKII) inhibits NHE3 by altering its trafficking and phosphorylating NHE3 at three required sites: Identification of a multifunctional phosphorylation site

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANES; MAMMALS; SIGNAL TRANSDUCTION; TITANIUM DIOXIDE;

EID: 84921683215     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.590174     Document Type: Article
Times cited : (47)

References (43)
  • 1
    • 0032736233 scopus 로고    scopus 로고
    • + exchanger NHE-3: Role of phosphorylation, protein trafficking, regulatory factors
    • + exchanger NHE-3: role of phosphorylation, protein trafficking, regulatory factors. J. Am. Soc. Nephrol. 10, 2412-2425
    • (1999) J. Am. Soc. Nephrol. , vol.10 , pp. 2412-2425
    • Moe, O.W.1
  • 2
    • 0030738872 scopus 로고    scopus 로고
    • + exchanger isoform 3 stably expressed in fibroblasts by fibroblast growth factor and phorbol esters is not through changes in phosphorylation of the exchanger
    • + exchanger isoform 3 stably expressed in fibroblasts by fibroblast growth factor and phorbol esters is not through changes in phosphorylation of the exchanger. J. Biol. Chem. 272, 18473-18480
    • (1997) J. Biol. Chem. , vol.272 , pp. 18473-18480
    • Yip, J.W.1    Ko, W.H.2    Viberti, G.3    Huganir, R.L.4    Donowitz, M.5    Tse, C.M.6
  • 4
    • 34548030449 scopus 로고    scopus 로고
    • NHE3 phosphorylation at serines 552 and 605 does not directly affect NHE3 activity
    • Kocinsky, H. S., Dynia, D. W., Wang, T., and Aronson, P. S. (2007) NHE3 phosphorylation at serines 552 and 605 does not directly affect NHE3 activity. Am. J. Physiol. Renal Physiol. 293, F212-F218
    • (2007) Am. J. Physiol. Renal Physiol. , vol.293 , pp. F212-F218
    • Kocinsky, H.S.1    Dynia, D.W.2    Wang, T.3    Aronson, P.S.4
  • 5
    • 0036196979 scopus 로고    scopus 로고
    • Structure and function of the heat-stable enterotoxin receptor/guanylyl cyclase C
    • Vaandrager, A. B. (2002) Structure and function of the heat-stable enterotoxin receptor/guanylyl cyclase C. Mol. Cell. Biochem. 230, 73-83
    • (2002) Mol. Cell. Biochem. , vol.230 , pp. 73-83
    • Vaandrager, A.B.1
  • 6
    • 0033976962 scopus 로고    scopus 로고
    • Differential role of cyclic GMP-dependent protein kinase II in ion transport in murine small intestine and colon
    • Vaandrager, A. B., Bot, A. G., Ruth, P., Pfeifer, A., Hofmann, F., and De Jonge, H. R. (2000) Differential role of cyclic GMP-dependent protein kinase II in ion transport in murine small intestine and colon. Gastroenterology 118, 108-114
    • (2000) Gastroenterology , vol.118 , pp. 108-114
    • Vaandrager, A.B.1    Bot, A.G.2    Ruth, P.3    Pfeifer, A.4    Hofmann, F.5    De Jonge, H.R.6
  • 7
    • 0031041098 scopus 로고    scopus 로고
    • Guanosine 3′,5′-cyclic monophosphate-dependent protein kinase II mediates heat-stable enterotoxin-provoked chloride secretion in rat intestine
    • Vaandrager, A. B., Bot, A. G., and De Jonge, H. R. (1997) Guanosine 3′,5′-cyclic monophosphate-dependent protein kinase II mediates heat-stable enterotoxin-provoked chloride secretion in rat intestine. Gastroenterology 112, 437-443
    • (1997) Gastroenterology , vol.112 , pp. 437-443
    • Vaandrager, A.B.1    Bot, A.G.2    De Jonge, H.R.3
  • 10
    • 0032491428 scopus 로고    scopus 로고
    • The role of NHERF and E3KARP in the cAMP-mediated inhibition of NHE3
    • Lamprecht, G., Weinman, E. J., and Yun, C. H. (1998) The role of NHERF and E3KARP in the cAMP-mediated inhibition of NHE3. J. Biol. Chem. 273, 29972-29978
    • (1998) J. Biol. Chem. , vol.273 , pp. 29972-29978
    • Lamprecht, G.1    Weinman, E.J.2    Yun, C.H.3
  • 23
    • 33744779069 scopus 로고    scopus 로고
    • The NHE3 juxtamembrane cytoplasmic domain directly binds ezrin: Dual role in NHE3 trafficking and mobility in the brush border
    • Cha, B., Tse, M., Yun, C., Kovbasnjuk, O., Mohan, S., Hubbard, A., Arpin, M., and Donowitz, M. (2006) The NHE3 juxtamembrane cytoplasmic domain directly binds ezrin: dual role in NHE3 trafficking and mobility in the brush border. Mol. Biol. Cell 17, 2661-2673
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2661-2673
    • Cha, B.1    Tse, M.2    Yun, C.3    Kovbasnjuk, O.4    Mohan, S.5    Hubbard, A.6    Arpin, M.7    Donowitz, M.8
  • 28
    • 0344514653 scopus 로고    scopus 로고
    • Dopamine acutely decreases apical membrane Na+/H+ exchanger NHE3 protein in mouse renal proximal tubule
    • Bacic, D., Kaissling, B., McLeroy, P., Zou, L., Baum, M., and Moe, O. W. (2003) Dopamine acutely decreases apical membrane Na+/H+ exchanger NHE3 protein in mouse renal proximal tubule. Kidney Int. 64, 2133-2141
    • (2003) Kidney Int. , vol.64 , pp. 2133-2141
    • Bacic, D.1    Kaissling, B.2    McLeroy, P.3    Zou, L.4    Baum, M.5    Moe, O.W.6
  • 29
    • 0035920227 scopus 로고    scopus 로고
    • + exchanger (NHE3) endocytosis via clathrin-coated vesicles: Dependence on protein kinase A-mediated NHE3 phosphorylation
    • + exchanger (NHE3) endocytosis via clathrin-coated vesicles: dependence on protein kinase A-mediated NHE3 phosphorylation. J. Biol. Chem. 276, 26906-26915
    • (2001) J. Biol. Chem. , vol.276 , pp. 26906-26915
    • Hu, M.C.1    Fan, L.2    Crowder, L.A.3    Karim-Jimenez, Z.4    Murer, H.5    Moe, O.W.6
  • 30
    • 0028031978 scopus 로고
    • N-[2-Bromocinnamyl (amino)ethyl]-5-isoquinolinesulphonamide (H-89) inhibits incorporation of choline into phosphatidylcholine via inhibition of choline kinase and has no effect on the phosphorylation of CTP:Phosphocholine cytidylyltransferase
    • Wieprecht, M., Wieder, T., and Geilen, C. C. (1994) N-[2-Bromocinnamyl (amino)ethyl]-5-isoquinolinesulphonamide (H-89) inhibits incorporation of choline into phosphatidylcholine via inhibition of choline kinase and has no effect on the phosphorylation of CTP:phosphocholine cytidylyltransferase. Biochem. J. 297, 241-247
    • (1994) Biochem. J. , vol.297 , pp. 241-247
    • Wieprecht, M.1    Wieder, T.2    Geilen, C.C.3
  • 31
    • 0036813656 scopus 로고    scopus 로고
    • Nitric oxide/cGMP-mediated protein kinase A activation in the antennal lobes plays an important role in appetitive reflex habituation in the honeybee
    • Müller, U., and Hildebrandt, H. (2002) Nitric oxide/cGMP-mediated protein kinase A activation in the antennal lobes plays an important role in appetitive reflex habituation in the honeybee. J. Neurosci. 22, 8739-8747
    • (2002) J. Neurosci. , vol.22 , pp. 8739-8747
    • Müller, U.1    Hildebrandt, H.2
  • 32
    • 34250156365 scopus 로고    scopus 로고
    • cAMP and cGMP signaling cross-talk: Role of phosphodiesterases and implications for cardiac pathophysiology
    • Zaccolo, M., and Movsesian, M. A. (2007) cAMP and cGMP signaling cross-talk: role of phosphodiesterases and implications for cardiac pathophysiology. Circ. Res. 100, 1569-1578
    • (2007) Circ. Res. , vol.100 , pp. 1569-1578
    • Zaccolo, M.1    Movsesian, M.A.2
  • 33
    • 0028866307 scopus 로고
    • Protein kinase A regulates the degradation rate of Rs acetylcholine receptors
    • Xu, R., and Salpeter, M. M. (1995) Protein kinase A regulates the degradation rate of Rs acetylcholine receptors. J. Cell. Physiol. 165, 30-39
    • (1995) J. Cell. Physiol. , vol.165 , pp. 30-39
    • Xu, R.1    Salpeter, M.M.2
  • 34
    • 0029155743 scopus 로고
    • + exchanger NHE-1 isoform in osteoblastic cells (UMR-106) via a cAMP-dependent pathway
    • + exchanger NHE-1 isoform in osteoblastic cells (UMR-106) via a cAMP-dependent pathway. J. Biol. Chem. 270, 23166-23172
    • (1995) J. Biol. Chem. , vol.270 , pp. 23166-23172
    • Azarani, A.1    Orlowski, J.2    Goltzman, D.3
  • 35
    • 0028936801 scopus 로고
    • Capacitation of mouse spermatozoa: II. Protein tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway
    • Visconti, P. E., Moore, G. D., Bailey, J. L., Leclerc, P., Connors, S. A., Pan, D., Olds-Clarke, P., and Kopf, G. S. (1995) Capacitation of mouse spermatozoa: II. protein tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway. Development 121, 1139-1150
    • (1995) Development , vol.121 , pp. 1139-1150
    • Visconti, P.E.1    Moore, G.D.2    Bailey, J.L.3    Leclerc, P.4    Connors, S.A.5    Pan, D.6    Olds-Clarke, P.7    Kopf, G.S.8
  • 36
    • 77649117952 scopus 로고    scopus 로고
    • Cooperativity within proximal phosphorylation sites is revealed from large-scale proteomics data
    • Schweiger, R., and Linial, M. (2010) Cooperativity within proximal phosphorylation sites is revealed from large-scale proteomics data. Biol. Direct. 26, 5-6
    • (2010) Biol. Direct. , vol.26 , pp. 5-6
    • Schweiger, R.1    Linial, M.2
  • 37
    • 0030175899 scopus 로고    scopus 로고
    • Characterization of multiple phosphorylation sites on the AMPA receptor GluR1 subunit
    • Roche, K. W., O'Brien, R. J., Mammen, A. L., Bernhardt, J., and Huganir, R. L. (1996) Characterization of multiple phosphorylation sites on the AMPA receptor GluR1 subunit. Neuron 16, 1179-1188
    • (1996) Neuron , vol.16 , pp. 1179-1188
    • Roche, K.W.1    O'Brien, R.J.2    Mammen, A.L.3    Bernhardt, J.4    Huganir, R.L.5
  • 40
    • 33846287933 scopus 로고    scopus 로고
    • Acute activation of NHE3 by dexamethasone correlates with activation of SGK1 and requires a functional glucocorticoid receptor
    • Wang, D., Zhang, H., Lang, F., and Yun, C. C. (2007) Acute activation of NHE3 by dexamethasone correlates with activation of SGK1 and requires a functional glucocorticoid receptor. Am. J. Physiol. Cell Physiol. 292, C396-C404
    • (2007) Am. J. Physiol. Cell Physiol. , vol.292 , pp. C396-C404
    • Wang, D.1    Zhang, H.2    Lang, F.3    Yun, C.C.4
  • 43
    • 34447629085 scopus 로고    scopus 로고
    • Regulatory binding partners and complexes of NHE3
    • Donowitz, M., and Li, X. (2007) Regulatory binding partners and complexes of NHE3. Physiol. Rev. 87, 825-872
    • (2007) Physiol. Rev. , vol.87 , pp. 825-872
    • Donowitz, M.1    Li, X.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.