FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W4281566614> ?p ?o ?g. }

• W4281566614 endingPage "119298" @default.
• W4281566614 startingPage "119298" @default.
• W4281566614 abstract "Calpain-5 (CAPN5) is a member of the calpain family of calcium-activated neutral thiol proteases. CAPN5 is partly membrane associated, despite its lack of a transmembrane domain. Unlike classical calpains, CAPN5 contains a C-terminal C2 domain. C2 domains often have affinity to lipids, mediating membrane association. We recently reported that the C2 domain of CAPN5 was essential for its membrane association and the activation of its autolytic activity. However, despite the removal of the C2 domain by autolysis, the N-terminal fragment of CAPN5 remained membrane associated. S-acylation, also referred to as S-palmitoylation, is a reversible post-translational lipid modification of cysteine residues that promotes membrane association of soluble proteins. In the present study several S-acylated cysteine residues were identified in CAPN5 with the acyl-PEG exchange method. Data reported here demonstrate that CAPN5 is S-acylated on up to three cysteine residues including Cys-4 and Cys-512, and likely Cys-507. The D589N mutation in a potential calcium binding loop within the C2 domain interfered with the S-acylation of CAPN5, likely preventing initial membrane association. Mutating specific cysteine residues of CAPN5 interfered with both its membrane association and the activation of CAPN5 autolysis. Taken together, our results suggest that the S-acylation of CAPN5 is critical for its membrane localization which appears to favor its enzymatic activity." @default.
• W4281566614 created "2022-05-27" @default.
• W4281566614 creator A5003994463 @default.
• W4281566614 creator A5035833348 @default.
• W4281566614 creator A5049575435 @default.
• W4281566614 creator A5066589887 @default.
• W4281566614 creator A5073393035 @default.
• W4281566614 creator A5090745009 @default.
• W4281566614 date "2022-09-01" @default.
• W4281566614 modified "2023-09-29" @default.
• W4281566614 title "S-acylation regulates the membrane association and activity of Calpain-5" @default.
• W4281566614 cites W1538162617 @default.
• W4281566614 cites W1803102843 @default.
• W4281566614 cites W1845946429 @default.
• W4281566614 cites W1867506901 @default.
• W4281566614 cites W1868380476 @default.
• W4281566614 cites W1940545045 @default.
• W4281566614 cites W1955249161 @default.
• W4281566614 cites W1968938163 @default.
• W4281566614 cites W1974372961 @default.
• W4281566614 cites W1975421091 @default.
• W4281566614 cites W1986160949 @default.
• W4281566614 cites W1988267551 @default.
• W4281566614 cites W1990524685 @default.
• W4281566614 cites W1991402029 @default.
• W4281566614 cites W1993009807 @default.
• W4281566614 cites W1993556675 @default.
• W4281566614 cites W1996225493 @default.
• W4281566614 cites W1997151018 @default.
• W4281566614 cites W1998917031 @default.
• W4281566614 cites W2002560793 @default.
• W4281566614 cites W2003597344 @default.
• W4281566614 cites W2003861021 @default.
• W4281566614 cites W2004438254 @default.
• W4281566614 cites W2008186920 @default.
• W4281566614 cites W2018127398 @default.
• W4281566614 cites W2022480984 @default.
• W4281566614 cites W2023100445 @default.
• W4281566614 cites W2025346060 @default.
• W4281566614 cites W2027045842 @default.
• W4281566614 cites W2034292153 @default.
• W4281566614 cites W2034512365 @default.
• W4281566614 cites W2040698692 @default.
• W4281566614 cites W2041471532 @default.
• W4281566614 cites W2045618968 @default.
• W4281566614 cites W2047613950 @default.
• W4281566614 cites W2048247819 @default.
• W4281566614 cites W2048559110 @default.
• W4281566614 cites W2049830397 @default.
• W4281566614 cites W2051808752 @default.
• W4281566614 cites W2055043387 @default.
• W4281566614 cites W2063559185 @default.
• W4281566614 cites W2063697444 @default.
• W4281566614 cites W2068347916 @default.
• W4281566614 cites W2069509382 @default.
• W4281566614 cites W2071606495 @default.
• W4281566614 cites W2073294726 @default.
• W4281566614 cites W2075929045 @default.
• W4281566614 cites W2078410070 @default.
• W4281566614 cites W2081095444 @default.
• W4281566614 cites W2081481124 @default.
• W4281566614 cites W2087354432 @default.
• W4281566614 cites W2087780172 @default.
• W4281566614 cites W2089178885 @default.
• W4281566614 cites W2090883317 @default.
• W4281566614 cites W2095914409 @default.
• W4281566614 cites W2108036428 @default.
• W4281566614 cites W2113901436 @default.
• W4281566614 cites W2114306774 @default.
• W4281566614 cites W2124792702 @default.
• W4281566614 cites W2129105333 @default.
• W4281566614 cites W2129544583 @default.
• W4281566614 cites W2143512531 @default.
• W4281566614 cites W2144052775 @default.
• W4281566614 cites W2145075118 @default.
• W4281566614 cites W2151014533 @default.
• W4281566614 cites W2160678789 @default.
• W4281566614 cites W2164571708 @default.
• W4281566614 cites W2167148836 @default.
• W4281566614 cites W2169436026 @default.
• W4281566614 cites W2173732482 @default.
• W4281566614 cites W2182059649 @default.
• W4281566614 cites W2252267431 @default.
• W4281566614 cites W2267906346 @default.
• W4281566614 cites W2271326832 @default.
• W4281566614 cites W2276124753 @default.
• W4281566614 cites W2319428081 @default.
• W4281566614 cites W2345734261 @default.
• W4281566614 cites W2421435187 @default.
• W4281566614 cites W2431193407 @default.
• W4281566614 cites W2466378003 @default.
• W4281566614 cites W2576479631 @default.
• W4281566614 cites W2590423871 @default.
• W4281566614 cites W2591801370 @default.
• W4281566614 cites W2598561739 @default.
• W4281566614 cites W2731898189 @default.
• W4281566614 cites W2731991504 @default.
• W4281566614 cites W2734199346 @default.

• next