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Gene Review:

SCAMP2 - secretory carrier membrane protein 2

Homo sapiens

Synonyms: Secretory carrier membrane protein 2, Secretory carrier-associated membrane protein 2

Müller, H.K. et al., Liu, L. et al., Wu, T.T. et al., Lin, P.J. et al., Guo, Z. et al., et al.

Castle, Guo, Liu,

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High impact information on SCAMP2

In addition, SERT was found to form a complex with SCAMP2 as demonstrated by co-immunoprecipitation from a heterologous expression system and from rat brain homogenate [1].
Subcellular redistribution of the serotonin transporter by secretory carrier membrane protein 2 [1].
These associations have been implicated in exocytosis by observing enhanced coIP of Arf6 with SCAMP2 after cell depolarization and in the presence of guanosine 5'-O-(3-thio)triphosphate and by inhibition of coIP by a SCAMP-derived peptide that inhibits exocytosis [2].
Thus, SCAMP2 couples Arf6-stimulated PLD activity to exocytosis and links this process to formation of fusion pores [2].
SCAMP2 interacts with Arf6 and phospholipase D1 and links their function to exocytotic fusion pore formation in PC12 cells [2].

Biological context of SCAMP2

Regulated overexpression of SCAMP2 with point mutations in its E peptide but not of normal SCAMP2 caused dose-dependent inhibition of depolarization-induced secretion [3].
Using the yeast two-hybrid approach we screened a human brain cDNA library and identified secretory carrier membrane protein 2 (SCAMP2) as a novel SERT-interacting protein [1].

Anatomical context of SCAMP2

An oligopeptide, E peptide, within the cytoplasmic segment linking the second and third transmembrane spans, particularly of SCAMP2, potently inhibits exocytosis in streptolysin O-permeabilized mast cells [4].
The two major size variants, SCAMP1 (37 kDa) and SCAMP2 (39 kDa), extensively colocalize in membranes of fibroblasts and parotid acinar cells based on immunocytochemistry and velocity centrifugation, although the relative amounts of each variant may differ in selected organelles [5].

Physical interactions of SCAMP2

Biochemical analyses indicated that the C-terminal cytoplasmic tail of NHE7 bound preferentially to a highly conserved cytoplasmic loop between the second and the third transmembrane segments (TM2-TM3 loop) of SCAMP2 [6].

Other interactions of SCAMP2

Taken together, our results suggest that SCAMP2 plays an important role in the regulation of the subcellular distribution of SERT [1].
Our recent findings implicate the SNAP receptor (SNARE) protein SNAP-23 and secretory carrier membrane protein 2 (SCAMP2) as regulators of this process [7].

References

Subcellular redistribution of the serotonin transporter by secretory carrier membrane protein 2. Müller, H.K., Wiborg, O., Haase, J. J. Biol. Chem. (2006) [Pubmed]
SCAMP2 interacts with Arf6 and phospholipase D1 and links their function to exocytotic fusion pore formation in PC12 cells. Liu, L., Liao, H., Castle, A., Zhang, J., Casanova, J., Szabo, G., Castle, D. Mol. Biol. Cell (2005) [Pubmed]
Role of secretory carrier membrane protein SCAMP2 in granule exocytosis. Liu, L., Guo, Z., Tieu, Q., Castle, A., Castle, D. Mol. Biol. Cell (2002) [Pubmed]
Perturbation of a very late step of regulated exocytosis by a secretory carrier membrane protein (SCAMP2)-derived peptide. Guo, Z., Liu, L., Cafiso, D., Castle, D. J. Biol. Chem. (2002) [Pubmed]
Evidence for colocalization and interaction between 37 and 39 kDa isoforms of secretory carrier membrane proteins (SCAMPs). Wu, T.T., Castle, J.D. J. Cell. Sci. (1997) [Pubmed]
Secretory carrier membrane proteins interact and regulate trafficking of the organellar (Na+,K+)/H+ exchanger NHE7. Lin, P.J., Williams, W.P., Luu, Y., Molday, R.S., Orlowski, J., Numata, M. J. Cell. Sci. (2005) [Pubmed]
Function of the t-SNARE SNAP-23 and secretory carrier membrane proteins (SCAMPs) in exocytosis in mast cells. Castle, J.D., Guo, Z., Liu, L. Mol. Immunol. (2002) [Pubmed]

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