2004
DOI: 10.1016/j.gene.2003.09.046
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Identification of Krit1B: a novel alternative splicing isoform of cerebral cavernous malformation gene-1

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Cited by 18 publications
(15 citation statements)
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References 71 publications
(104 reference statements)
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“…A KRIT1A-expresssing lentiviral construct was generated from the HIV-derived self-inactivating transfer construct pCCLsin.PPT.PGK.EGFP.Wpre (provided by L. Naldini, HSR-TIGET) by replacing the GFP cassette with the murine KRIT1A cDNA [127]. Lentiviral vector particles were produced in 293T packaging cells, transiently cotransfected with a mix of transfer, envelope, and core-packaging constructs, as described previously [31].…”
Section: Methodsmentioning
confidence: 99%
“…A KRIT1A-expresssing lentiviral construct was generated from the HIV-derived self-inactivating transfer construct pCCLsin.PPT.PGK.EGFP.Wpre (provided by L. Naldini, HSR-TIGET) by replacing the GFP cassette with the murine KRIT1A cDNA [127]. Lentiviral vector particles were produced in 293T packaging cells, transiently cotransfected with a mix of transfer, envelope, and core-packaging constructs, as described previously [31].…”
Section: Methodsmentioning
confidence: 99%
“…pLVX-KRIT1 overexpression vector was obtained by subcloning the KRIT1 cDNA cassette [24] into the pLVX lentiviral expression vector (Clontech Laboratories, Mountain View, CA). The human miR-21 gene was amplified from HeLa genomic DNA and cloned into the pWPT lentivirus vector (Addgene, Cambridge, MA) to obtain pWPT-miR-21.The luciferase reporter vector containing a partial portion (973 nts, positions 340–1313) of the human KRIT1 3′UTR was generated by PCR amplification from HeLa genomic DNA, cloned downstream of the luciferase coding sequence into the pMIR-REPORT™ vector (Ambion, Austin, TX).…”
Section: Methodsmentioning
confidence: 99%
“…In a previous work we identified a novel KRIT1 isoform, KRIT1B, characterized by the alternative splicing of the 15th coding exon, which results in a 117-bp in-frame deletion accounting for the exclusion of 39 aa in a region close to C-terminus of full-length KRIT1A [24]. The alternative splicing affects the β sandwich of the F3/PTB lobe of the KRIT1 FERM domain.…”
Section: Resultsmentioning
confidence: 99%
“…On the other hand, we previously identified a second KRIT1 isoform, KRIT1B, characterized by the alternative splicing of the 15th coding exon, which results in a shorter protein lacking 39 aa in the C-terminus [24]. We found that the alternative splicing strongly affects the structure of the F3/PTB lobe of the KRIT1 FERM domain with important functional implications, including the loss of the ability to undertake head-to-tail intramolecular interaction, binding to Rap1 and nucleocytoplasmic shuttling.…”
Section: Introductionmentioning
confidence: 99%