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首页> 外文期刊>Journal of Molecular Biology >The molecular basis of the Caskin1 and Mint1 interaction with CASK.
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The molecular basis of the Caskin1 and Mint1 interaction with CASK.

机译：Caskin1和Mint1与CASK相互作用的分子基础。

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Calcium/calmodulin-dependent serine protein kinase (CASK) is a conserved multi-domain scaffolding protein involved in brain development, synapse formation, and establishment of cell polarity. To accomplish these diverse functions, CASK participates in numerous protein-protein interactions. In particular, CASK forms competing CASK/Mint1/Velis and CASK/Caskin1/Velis tripartite complexes that physically associate with the cytoplasmic tail of neurexin, a transmembrane protein enriched at presynaptic sites. This study shows that a short linear EEIWVLRK peptide motif from Caskin1 is necessary and sufficient for binding CASK. We also identified the conserved binding site for the peptide on the CASK calmodulin kinase domain. A related EPIWVMRQ peptide from Mint1 was also discovered to be sufficient for binding. Searching all human proteins for the Mint1/Caskin1 consensus peptide ExIWVxR revealed that T-cell lymphoma invasion and metastasis 1 (TIAM1) contains a conserved EEVIWVRRE peptide that was also found to be sufficient for CASK binding in vitro. TIAM1 is well known for its role in tumor metastasis, but it also possesses overlapping cellular and neurological functions with CASK, suggesting a previously unknown cooperation between the two proteins. This new peptide interaction motif also explains how Caskin1 and Mint1 form competing complexes and suggests a new role for the cellular hub protein CASK.
机译：钙/钙调蛋白依赖性丝氨酸蛋白激酶（CASK）是一种保守的多域支架蛋白，参与大脑发育，突触形成和细胞极性的建立。为了完成这些多样化的功能，CASK参与了许多蛋白质-蛋白质相互作用。特别是，CASK形成了竞争性的CASK / Mint1 / Velis和CASK / Caskin1 / Velis三方复合物，它们与神经营养素（突触前位点富集的跨膜蛋白）的胞质尾端物理结合。这项研究表明，Caskin1的短线性EEIWVLRK肽基序对于结合CASK是必要和充分的。我们还确定了CASK钙调蛋白激酶域上该肽的保守结合位点。还发现来自Mint1的相关EPIWVMRQ肽足以结合。在所有人类蛋白质中搜索Mint1 / Caskin1共有肽ExIWVxR，发现T细胞淋巴瘤侵袭和转移1（TIAM1）包含一个保守的EEVIWVRRE肽，该肽也足以在体外与CASK结合。 TIAM1因其在肿瘤转移中的作用而闻名，但它也具有与CASK重叠的细胞和神经功能，表明这两种蛋白之间以前未知的合作。这种新的肽相互作用基序还解释了Caskin1和Mint1如何形成竞争复合物，并暗示了细胞中心蛋白CASK的新作用。

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