期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 283, 期 4, 页码 1848-1856出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M708044200
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资金
- NCRR NIH HHS [P41 RR006009] Funding Source: Medline
- NIAID NIH HHS [R01 AI038282, R21 AI044902, R01 AI044902, R01 AI44902, R01 AI38282] Funding Source: Medline
- NIGMS NIH HHS [R01 GM051338, R01 GM51338] Funding Source: Medline
Micropipette manipulation measurements quantified the pre-steady state binding kinetics between cell pairs mediated by Xenopus cleavage stage cadherin. The time-dependence of the intercellular binding probability exhibits a fast forming, low probability binding state, which transitions to a slower forming, high probability state. The biphasic kinetics are independent of the cytoplasmic region, but the transition to the high probability state requires the third extracellular domain EC3. Deleting either EC3 or EC3-5, or substituting Trp(2) for Ala reduces the binding curves to a simple, monophasic rise in binding probability to a limiting plateau, as predicted for a single site binding mechanism. The two stage cadherin binding process reported here directly parallels previous biophysical studies, and confirms that the cadherin ectodomain governs the initial intercellular adhesion dynamics.
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