N-terminal signal sequence is required for cellular trafficking and hyaluronan-depolymerization of KIAA1199
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- 作者：Hiroyuki Yoshida ; Aya Nagaoka ; Sachiko Nakamura ; Megumi Tobiishi ; Yoshinori Sugiyama ; Shintaro Inoue
- 关键词：HA ; hyaluronan ; HYAL ; hyaluronidase ; ORF ; open reading frame ; ER ; endoplasmic reticulum ; HEK ; human embryonic kidney ; FBS ; fetal bovine serum ; FA ; fluoresceinamine ; GAPDH ; glyceraldehyde 3-phosphate dehydrogenase ; LDS ; lithium dodecyl sulfate ; SDS ; sodium dodecyl sulfate ; CPC ; cetylpyridinium chloride ; PBS ; phosphate-buffered saline ; PBS-T ; PBS containing 0.05% (vol/vol) Tween 20 ; DMEM ; Dulbecco&rsquo ; s Modified Eagle&rsquo ; s Medium ; Endo H ; endo-尾-N-acetylglucosaminidase H ; DTT ; dithiothreitol
- 刊名：FEBS Letters
- 出版年：3 January, 2014
- 年：2014
- 卷：588
- 期：1
- 页码：111-116
- 全文大小：1065 K
文摘
Recently, we disclosed that KIAA1199-mediated hyaluronan (HA) depolymerization requires an acidic cellular microenvironment (e.g. clathrin-coated vesicles or early endosomes), but no information about the structural basis underlying the cellular targeting and functional modification of KIAA1199 was available. Here, we show that the cleavage of N-terminal 30 amino acids occurs in functionally matured KIAA1199, and the deletion of the N-terminal portion results in altered intracellular trafficking of the molecule and loss of cellular HA depolymerization. These results suggest that the N-terminal portion of KIAA1199 functions as a cleavable signal sequence required for proper KIAA1199 translocation and KIAA1199-mediated HA depolymerization.