Department of Pharmacology and Physiology, New Jersey Medical School, University of Medicine and Dentistry of New Jersey, Newark, NJ 07103, USA.
Biochem J. 2009 Dec 10;424(3):385-98. doi: 10.1042/BJ20091140.
Gap junctions play important roles in auditory function and skin biology; mutations in the Cx26 (connexin26) gene are the predominant cause of inherited non-syndromic deafness and cause disfiguring skin disorders. Mass spectrometry (MS) was used to identify PTMs (post-translational modifications) of Cx26 and to determine whether they occur at sites of disease-causing mutations. Cx26 was isolated from transfected HeLa cells by sequential immunoaffinity and metal chelate chromatography using a tandem C-terminal haemagglutinin epitope and a (His-Asn)6 sequence. In-gel and in-solution enzymatic digestions were carried out in parallel with trypsin, chymotrypsin and endoproteinase GluC. Peptides were fractionated using a reversed-phase matrix by stepwise elution with increasing concentrations of organic solvent. To improve detection of low-abundance peptides and to maximize sequence coverage, MALDI-TOF-MS (matrix-assisted laser desorption/ionization-time-of-flight mass spectrometry; MS) and MALDI-TOF/TOF-MS/MS (matrix-assisted laser desorption/ionization-time-of-flight/time-of-flight tandem mass spectrometry; MS/MS) spectra were acquired from each elution step using an Applied Biosystems 4800 tandem mass spectrometer. Acquisition, processing and interpretation parameters were optimized to improve ionization and fragmentation of hydrophobic peptides. MS and MS/MS coverage of Cx26 was significantly above that reported for other membrane proteins: 71.3% by MS, with 29.9% by MS/MS. MS coverage was 92.6% if peptides resulting from in-source collisions and/or partial enzymatic cleavages were considered. A variety of putative PTMs of Cx26 were identified, including acetylation, hydroxylation, gamma-carboxyglutamation, methylation and phosphorylation, some of which are at sites of deafness-causing mutations. Knowledge of the PTMs of Cx26 will be instrumental in understanding how alterations in the cellular mechanisms of Cx26 channel biogenesis and function lead to losses in auditory function and disfiguring skin disorders.
缝隙连接在听觉功能和皮肤生物学中发挥着重要作用;Cx26(连接蛋白 26)基因的突变是遗传性非综合征性耳聋的主要原因,并导致毁容性皮肤疾病。质谱(MS)用于鉴定 Cx26 的翻译后修饰(PTMs),并确定它们是否发生在致病突变部位。Cx26 从转染的 HeLa 细胞中通过顺序免疫亲和和金属螯合层析分离,使用串联 C 末端血凝素表位和(His-Asn)6 序列。在凝胶内和溶液中平行进行胰蛋白酶、糜蛋白酶和内切蛋白酶 GluC 的酶消化。肽使用反相基质通过逐步用有机溶剂的浓度增加进行洗脱进行分离。为了提高低丰度肽的检测率并最大限度地提高序列覆盖率,使用 Applied Biosystems 4800 串联质谱仪从每个洗脱步骤采集 MALDI-TOF-MS(基质辅助激光解吸/电离-飞行时间质谱;MS)和 MALDI-TOF/TOF-MS/MS(基质辅助激光解吸/电离-飞行时间/飞行时间串联质谱;MS/MS)谱。优化了采集、处理和解释参数,以改善疏水性肽的电离和碎裂。Cx26 的 MS 和 MS/MS 覆盖率明显高于其他膜蛋白:MS 为 71.3%,MS/MS 为 29.9%。如果考虑到源自源内碰撞和/或部分酶切的肽,则 MS 覆盖率为 92.6%。鉴定出 Cx26 的多种假定 PTMs,包括乙酰化、羟化、γ-羧化、甲基化和磷酸化,其中一些发生在致聋突变部位。了解 Cx26 的 PTMs 将有助于理解 Cx26 通道生物发生和功能的细胞机制的改变如何导致听觉功能丧失和毁容性皮肤疾病。