gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 08 Dec 2016.

Trafficking protein particle complex 2

SEDL, SEDT, sedlin
The protein encoded by this gene is thought to be part of a large multi-subunit complex involved in the targeting and fusion of endoplasmic reticulum-to-Golgi transport vesicles with their acceptor compartment. In addition, the encoded protein can bind c-myc promoter-binding protein 1 and block its transcriptional repression capability. Mutations in this gene are a cause of spondyloepiphyseal dysplasia tarda (SEDT). A processed pseudogene of this gene is located on chromosome 19, and other pseudogenes are found on chromosomes 8 and Y. Alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Mar 2010] (from NCBI)
Papers on SEDL
Sedlin controls the ER export of procollagen by regulating the Sar1 cycle.
De Matteis et al., Napoli, Italy. In Science, 2012
Sedlin bound and promoted efficient cycling of Sar1, a guanosine triphosphatase that can constrict membranes, and thus allowed nascent carriers to grow and incorporate procollagen prefibrils.
A yeast two hybrid screen identifies SPATA4 as a TRAPP interactor.
Sacher et al., Montréal, Canada. In Febs Lett, 2011
Data indicate SPATA4 interacts with the C2 portion of the TRAPP complex.
The adaptor function of TRAPPC2 in mammalian TRAPPs explains TRAPPC2-associated SEDT and TRAPPC9-associated congenital intellectual disability.
Yu et al., Hong Kong, Hong Kong. In Plos One, 2010
Data show that a disease-causing mutation of TRAPPC2, D47Y, failed to interact with either TRAPPC9 or TRAPPC8, suggesting that aspartate 47 in TRAPPC2 is at or near the site of interaction with TRAPPC9 or TRAPPC8.
Interaction of Sedlin with PAM14.
Fan et al., Hefei, China. In J Cell Biochem, 2010
The results suggest that nucleus-localized Sedlin may play a role in regulation of transcriptional activities of the MRG family of transcription factors via binding to PAM14.
SEDLIN forms homodimers: characterisation of SEDLIN mutations and their interactions with transcription factors MBP1, PITX1 and SF1.
Thakker et al., Oxford, United Kingdom. In Plos One, 2009
SEDLIN is present in the nucleus, forms homodimers and that SEDT-associated mutations cause a loss of interaction with the transcription factors MBP1, PITX1 and SF1.
share on facebooktweetadd +1mail to friends