Limits...
The CacyBP/SIP protein is sumoylated in neuroblastoma NB2a cells.

Wasik U, Filipek A - Neurochem. Res. (2013)

Bottom Line: In this work we examined a post-translational modification of CacyBP/SIP which might have an effect on its function.By fractionation of NB2a cell extract we have found that, contrary to the majority of SUMO-modified proteins, sumoylated CacyBP/SIP is present in the cytoplasmic and not in the nuclear fraction.We have also established that lysine 16 is the residue which undergoes sumoylation in the CacyBP/SIP protein.

View Article: PubMed Central - PubMed

ABSTRACT
The Calcyclin binding protein and Siah-1 interacting protein (CacyBP/SIP) protein is highly expressed in mammalian brain as well as in neuroblastoma NB2a cells and pheochromocytoma PC12 cells. This protein interacts with several targets such as cytoskeletal proteins or ERK1/2 kinase and seems to be involved in many cellular processes. In this work we examined a post-translational modification of CacyBP/SIP which might have an effect on its function. Since theoretical analysis of the amino acid sequence of CacyBP/SIP indicated several lysine residues which could potentially be sumoylated we checked experimentally whether this protein might be modified by SUMO attachment. We have shown that indeed CacyBP/SIP bound the E2 SUMO ligase, Ubc9, in neuroblastoma NB2a cell extract and was sumoylated in these cells. By fractionation of NB2a cell extract we have found that, contrary to the majority of SUMO-modified proteins, sumoylated CacyBP/SIP is present in the cytoplasmic and not in the nuclear fraction. We have also established that lysine 16 is the residue which undergoes sumoylation in the CacyBP/SIP protein.

Show MeSH

Related in: MedlinePlus

The amino acid sequence of mouse CacyBP/SIP (accession number NP_033916). Lysine residues, identified by SUMOsp 2.0 tool, which might be potentially sumoylated are marked in bold (these with high probability) or underlined (these with lower probability)
© Copyright Policy - OpenAccess
Related In: Results  -  Collection


getmorefigures.php?uid=PMC3824344&req=5

Fig1: The amino acid sequence of mouse CacyBP/SIP (accession number NP_033916). Lysine residues, identified by SUMOsp 2.0 tool, which might be potentially sumoylated are marked in bold (these with high probability) or underlined (these with lower probability)

Mentions: The CacyBP/SIP amino acid sequence was analyzed by the SUMOsp 2.0 online tool (http://sumosp.biocuckoo.org). As it is shown in Fig. 1, several potential sumoylation sites were identified. Among them were lysine residues in positions 16, 37, 43, 49, 52, 53, 147 and 208.Fig. 1


The CacyBP/SIP protein is sumoylated in neuroblastoma NB2a cells.

Wasik U, Filipek A - Neurochem. Res. (2013)

The amino acid sequence of mouse CacyBP/SIP (accession number NP_033916). Lysine residues, identified by SUMOsp 2.0 tool, which might be potentially sumoylated are marked in bold (these with high probability) or underlined (these with lower probability)
© Copyright Policy - OpenAccess
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3824344&req=5

Fig1: The amino acid sequence of mouse CacyBP/SIP (accession number NP_033916). Lysine residues, identified by SUMOsp 2.0 tool, which might be potentially sumoylated are marked in bold (these with high probability) or underlined (these with lower probability)
Mentions: The CacyBP/SIP amino acid sequence was analyzed by the SUMOsp 2.0 online tool (http://sumosp.biocuckoo.org). As it is shown in Fig. 1, several potential sumoylation sites were identified. Among them were lysine residues in positions 16, 37, 43, 49, 52, 53, 147 and 208.Fig. 1

Bottom Line: In this work we examined a post-translational modification of CacyBP/SIP which might have an effect on its function.By fractionation of NB2a cell extract we have found that, contrary to the majority of SUMO-modified proteins, sumoylated CacyBP/SIP is present in the cytoplasmic and not in the nuclear fraction.We have also established that lysine 16 is the residue which undergoes sumoylation in the CacyBP/SIP protein.

View Article: PubMed Central - PubMed

ABSTRACT
The Calcyclin binding protein and Siah-1 interacting protein (CacyBP/SIP) protein is highly expressed in mammalian brain as well as in neuroblastoma NB2a cells and pheochromocytoma PC12 cells. This protein interacts with several targets such as cytoskeletal proteins or ERK1/2 kinase and seems to be involved in many cellular processes. In this work we examined a post-translational modification of CacyBP/SIP which might have an effect on its function. Since theoretical analysis of the amino acid sequence of CacyBP/SIP indicated several lysine residues which could potentially be sumoylated we checked experimentally whether this protein might be modified by SUMO attachment. We have shown that indeed CacyBP/SIP bound the E2 SUMO ligase, Ubc9, in neuroblastoma NB2a cell extract and was sumoylated in these cells. By fractionation of NB2a cell extract we have found that, contrary to the majority of SUMO-modified proteins, sumoylated CacyBP/SIP is present in the cytoplasmic and not in the nuclear fraction. We have also established that lysine 16 is the residue which undergoes sumoylation in the CacyBP/SIP protein.

Show MeSH
Related in: MedlinePlus