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Phosphorylation of Rab GTPases in the regulation of membrane trafficking.
Traffic ( IF 4.5 ) Pub Date : 2020-09-24 , DOI: 10.1111/tra.12765
Dieter Waschbüsch 1 , Amir R Khan 1, 2
Affiliation  

Rab GTPases are master regulators of membrane trafficking in eukaryotic cells. Phosphorylation of Rab GTPases was characterized in the 1990s and there have been intermittent reports of its relevance to Rab functions. Phosphorylation as a regulatory mechanism has gained prominence through the identification of Rabs as physiological substrates of leucine‐rich repeat kinase 2 (LRRK2). LRRK2 is a Ser/Thr kinase that is associated with inherited and sporadic forms of Parkinson disease. In recent years, numerous kinases and their associated signaling pathways have been identified that lead to phosphorylation of Rabs. These emerging studies suggest that serine/threonine and tyrosine phosphorylation of Rabs may be a widespread and under‐appreciated mechanism for controlling their membrane trafficking functions. Here we survey current knowledge of Rab phosphorylation and discuss models for how this post‐translational mechanism exerts control of membrane trafficking.

中文翻译:

Rab GTPases的磷酸化可调节膜运输。

Rab GTPases是真核细胞膜运输的主要调节剂。Rab GTPases的磷酸化的特征是在1990年代,并且断断续续地报道了其与Rab功能的相关性。通过将Rabs鉴定为富含亮氨酸的重复激酶2(LRRK2)的生理底物,磷酸化作为一种​​调节机制得到了重视。LRRK2是一种Ser / Thr激酶,与帕金森氏病的遗传和散发形式有关。近年来,已鉴定出导致Rabs磷酸化的众多激酶及其相关信号传导途径。这些新兴的研究表明,Rabs的丝氨酸/苏氨酸和酪氨酸磷酸化可能是控制其膜运输功能的普遍且未被充分认识的机制。
更新日期:2020-11-09
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