Transmembrane auxin carrier systems - dynamic regulators of polar auxin transport
Transmembrane auxin carrier systems - dynamic regulators of polar auxin transport
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DOI：
10.1023/a:1010701527848
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发表时间：
2000-11-01
影响因子：
4.2
通讯作者：
Morris, DA
中科院分区：
文献类型：
--
作者：
Morris, DA
最近对生长素极性运输的生物化学、生理学和分子遗传学的研究极大地促进了我们对生长素极性运输过程及其在发育调节和细胞、组织和器官对内部和外部刺激的反应中所起作用的理解。在极性生长素运输中表现出损伤的突变体的分子和生理学表征已经导致编码生长素载体系统的推定组分的基因或直接或间接调节这些系统的蛋白质的分离和测序。这项工作揭示了特定的生长素吸收和流出载体不是由单个基因编码，而是由整个基因家族编码，其表达是组织或刺激特异性的。此外，证据正在迅速积累，至少生长素外排载体是一个多组分系统，包括催化和调节亚基，包括一个单独的植物生长素结合蛋白。已经初步鉴定了编码调节编码生长素载体组分的基因的表达或调节生长素载体的细胞内运输或活性的蛋白质的其它基因。调查的周转和高尔基体介导的运输生长素载体蛋白已经揭示，至少外排载体的基本组成部分有一个非常短的半衰期在质膜和更换，而不需要同时蛋白质合成，导致推测，他们可能会循环之间的内部存储和质膜。现在的方式是明确的发展，具体的分子探针，研究细胞内运输和定位生长素载体蛋白。
Recent investigations of the biochemistry, physiology and molecular genetics of polar auxin transport have greatly advanced our understanding of the process and of the part it plays in the regulation of development and in the responses of cells, tissues and organs to internal and external stimuli. The molecular and physiological characterization of mutants which exhibit lesions in polar auxin transport has led to the isolation and sequencing of genes which encode putative components of auxin carrier systems, or proteins which directly or indirectly regulate these systems. This work has revealed that specific auxin uptake and efflux carriers are coded not by single genes, but by whole families of genes, the expression of which is tissue or stimulus specific. Furthermore, evidence is accumulating rapidly that at least the auxin efflux carrier is a multi-component system consisting of both catalytic and regulatory subunits, including a separate phytotropin-binding protein. Other genes have been tentatively identified which code proteins that regulate the expression of genes coding auxin carrier components, or which regulate the intracellular traffic or activity of auxin carriers. Investigations of the turn-over and Golgi-mediated trafficking of auxin carrier proteins have revealed that essential components of at least the efflux carrier have a very short half-life in the plasma membrane and are replaced without the need for concurrent protein synthesis, leading to speculation that they might cycle between internal stores and the plasma membrane. The way is now clear for the development of specific molecular probes with which to investigate the intracellular transport and targeting of auxin carrier proteins.