Paralemmin, a prenyl-palmitoyl-anchored phosphoprotein abundant in neurons and implicated in plasma membrane dynamics and cell process formation.
Paralemmin, a prenyl-palmitoyl-anchored phosphoprotein abundant in neurons and implicated in plasma membrane dynamics and cell process formation.
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Paralemmin 是一种异戊二烯基棕榈酰锚定磷蛋白，在神经元中含量丰富，与质膜动力学和细胞过程形成有关。
DOI：
10.1083/jcb.143.3.795
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发表时间：
1998-11-02
期刊：
影响因子：
--
通讯作者：
Kilimann MW
中科院分区：
文献类型：
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作者：
Kutzleb C;Sanders G;Yamamoto R;Wang X;Lichte B;Petrasch-Parwez E;Kilimann MW
我们报告的鉴定和初步表征的Eschemmin，一个假定的新的形态调节蛋白与质膜。Paralemmin在大脑中高度表达，但在许多其他组织和细胞类型中也不太丰富。来自鸡、人和小鼠的cDNA预测42 kD的酸性蛋白质，其显示由保守性差的接头序列分离的具有高度种间保守性的序列盒模式。三个半胱氨酸残基的COOH末端簇的异戊烯基化和棕榈酰化赋予Escheremmin疏水性和膜缔合。Paralemmin也被磷酸化，其mRNA以组织特异性和发育调节的方式差异剪接。差异剪接、脂质化和磷酸化导致电泳异质性，导致蛋白质印迹上出现一系列多条带，最明显的是在脑中。Paralemmin与突触后特化、轴突和树突过程和胞体的质膜的细胞质面相关，并且似乎也与细胞内囊泡池相关。它不是连续地排列在神经元质膜上，而是成簇和斑块状排列。它的分子和形态学性质使人联想到GAP-43、CAP-23和MARCKS，这些蛋白质与质膜动力学有关。在几种细胞系中的过表达表明，Escheremmin集中在质膜活性位点，如丝状伪足和微刺，并诱导细胞扩增和突起形成。脂化基序对于这种形态发生活性是必不可少的。我们提出了一个函数，用于控制细胞形状，例如，通过参与膜流动或膜-细胞骨架相互作用。
We report the identification and initial characterization of paralemmin, a putative new morphoregulatory protein associated with the plasma membrane. Paralemmin is highly expressed in the brain but also less abundantly in many other tissues and cell types. cDNAs from chicken, human, and mouse predict acidic proteins of 42 kD that display a pattern of sequence cassettes with high inter-species conservation separated by poorly conserved linker sequences. Prenylation and palmitoylation of a COOH-terminal cluster of three cysteine residues confers hydrophobicity and membrane association to paralemmin. Paralemmin is also phosphorylated, and its mRNA is differentially spliced in a tissue-specific and developmentally regulated manner. Differential splicing, lipidation, and phosphorylation contribute to electrophoretic heterogeneity that results in an array of multiple bands on Western blots, most notably in brain. Paralemmin is associated with the cytoplasmic face of the plasma membranes of postsynaptic specializations, axonal and dendritic processes and perikarya, and also appears to be associated with an intracellular vesicle pool. It does not line the neuronal plasmalemma continuously but in clusters and patches. Its molecular and morphological properties are reminiscent of GAP-43, CAP-23, and MARCKS, proteins implicated in plasma membrane dynamics. Overexpression in several cell lines shows that paralemmin concentrates at sites of plasma membrane activity such as filopodia and microspikes, and induces cell expansion and process formation. The lipidation motif is essential for this morphogenic activity. We propose a function for paralemmin in the control of cell shape, e.g., through an involvement in membrane flow or in membrane–cytoskeleton interaction.