The inner world of cell adhesion: integrin cytoplasmic domains.
The inner world of cell adhesion: integrin cytoplasmic domains.
复制标题
细胞粘附的内部世界：整合素胞质结构域。
DOI：
10.1016/0962-8924(94)90059-0
复制
发表时间：
1994
影响因子：
19
通讯作者：
M. Ginsberg
中科院分区：
文献类型：
--
作者：
Michael J. Williams;Paul E. Hughes;T. O’Toole;M. Ginsberg
细胞与环境之间的许多相互作用是由异二聚体跨膜受体整合素家族介导的。在过去的十年里，人们已经做出了广泛的努力来破译整合蛋白的功能。整合素结合细胞内和细胞外的配体，从而在两个方向上跨膜传递信号。这些受体的细胞质结构域在这种双向信息流动和细胞内外蛋白质结构之间直接物理联系的形成中起着关键作用。导致一个组成活性受体，而截断保留基序没有t‘, v’。此外，从OClll嵌合体中缺失VGFFK，并且细胞质结构域为0q。也把受体调高了。与细胞类型、细胞代谢和~胞质结构域TM截断无关的亲和状态。这些数据表明，GFFKR有助于维持低违约水平。亲和力的状态。对0 ~ 2、0 . 4和6个截断的研究结果表明，GFFKR c端上的序列可能介导13t整合素的生理“激活”17-19。然而，at~ 32在COS细胞中表达时具有组成性活性，at的部分缺失。细胞质结构域似乎对icam - 1的粘附没有影响（参考文献20,21）。嵌合整合素。不同细胞质结构域融合到OCnl的跨膜和胞外结构域的研究，13:（参考文献）。7)，证明了不同at亚基的细胞质结构域可以指定细胞。特定于类型的亲和状态。此外，~ 1和J3~的细胞质结构域也需要维持嵌合受体的高亲和力状态7。这与其他细胞质结构域的截断通过整合素2 ' '22导致细胞粘附减少的观察结果一致。有趣的是，细胞质结构域的Ser752 - Pro点突变破坏了“内向外”信号通路t " L
Many of the interactions between cells and their environment are mediated by the integrin family of heterodimeric transmembrane receptors. The past decade has seen a broad-based effort to decipher the roles by whiclz integrins function. Integrins bind both intracellular and extracellular iigands and thus transfer signals across the membrane in both directions. The cytoplasmic domains of these receptors play a key role in this bidirectional flow of infonnation and in the formation of direct physical linkages between protein structures on the inside and outside of the cell. resulted in a constitutively active receptor, whereas a truncation that preserved the motif did not t', v'. Moreover, deletion of VGFFK from a chimera of OClll, and the cytoplasmic domain of 0q. also switched the receptor into a high. affinity state that was independent of cell type, cellular metabolism and truncations of the~ cytoplasmic domain TM. These data suggest that GFFKR helps maintain a default low. affinity state. Results from studies of o~ 2, o. 4 and at 6 truncations suggest that sequences on the C-terminal side of the GFFKR may mediate physiological'activation'of 13 t integrins 17-19. However, at~ 32 is constitutively active when expressed in COS cells, and partial deletions of the at]. cytoplasmic domain appear to have no effect on adhesion to ICAM-I (Refs 20, 21). Chimeric integrins, compo~. ed of various cytoplasmic domains fused to the transmembrane and extracellular domains of OCnl, 13:(Ref. 7), demonstrated that the cytoplasmic domains of different at subunits can specify cell. type-specific affinity states. In addition, the cytoplasmic domains of~ 1 and J3~ were required to maintain the chimeric receptors in the high-affinity state 7. This is consistent with the observation that truncations of other~ cytoplasmic domains result in a reduction of cell adhesion through integrins 2"'22. Interestingly, an,~ turally occurring point mutation, Ser752 to Pro in the~ cytoplasmic domain, disrupts' inside-out'signallingT''L
登录
查看更多内容
DOI：
10.1016/s0021-9258(19)36909-1
发表时间：
1993-10
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
C. Otey;G. Vásquez;K. Burridge;B. W. Erickson
通讯作者：
C. Otey;G. Vásquez;K. Burridge;B. W. Erickson
影响因子：
56.9
作者：
HIBBS, ML;XU, H;SPRINGER, TA
通讯作者：
SPRINGER, TA
人血小板糖蛋白 IIIa (GPIIIa) 的磷酸化。
DOI：
--
发表时间：
1991
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Hillery,CA;Smyth,SS;Parise,LV
通讯作者：
Parise,LV
DOI：
10.1016/s0021-9258(18)42050-9
发表时间：
1992-08
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
J. Weisel;C. Nagaswami;G. Vilaire;J. Bennett
通讯作者：
J. Weisel;C. Nagaswami;G. Vilaire;J. Bennett
影响因子：
20.3
作者：
Susan S. Smyth;C. Joneckis;L. Parise
通讯作者：
Susan S. Smyth;C. Joneckis;L. Parise