Novel insights into the function of the conserved domain of the CAP superfamily of proteins

Nick K. Olrichs; J. Bernd Helms; Nick K. Olrichs; J. Bernd Helms

doi:10.3934/biophy.2016.2.232

AIMS Biophysics

2016, Volume 3, Issue 2: 232-246. doi: 10.3934/biophy.2016.2.232

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Novel insights into the function of the conserved domain of the CAP superfamily of proteins

Nick K. Olrichs ,
J. Bernd Helms ^,

Department of Biochemistry & Cell Biology and Institute of Biomembranes, Utrecht University, Utrecht, The Netherlands

Received: 16 March 2016 Accepted: 18 April 2016 Published: 21 April 2016

Members of the Cysteine-rich secretory proteins, Antigen 5, and Pathogenesis-related 1 proteins (CAP) superfamily are found in a remarkable variety of biological species. The presence of a highly conserved CAP domain defines the CAP family members, which in many cases is linked to other functional protein domains. As a result, this superfamily of proteins is involved in a large variety of biological processes such as reproduction, tumor suppression, and immune regulation. The role of the CAP domain and its conserved structure throughout evolution in relation to the diverse functions of CAP proteins is, however, poorly understood. Recent studies on the mammalian Golgi-Associated plant Pathogenesis Related protein 1 (GAPR-1), which consists almost exclusively of a CAP domain, may shed new light on the function of the CAP domain. GAPR-1 was shown to form amyloid fibrils but also to possess anti-amyloidogenic properties against other amyloid forming peptides. Amyloid prediction analysis reveals the presence of potentially amyloidogenic sequences within the highly conserved sequence motifs of the CAP domain. This review will address the structural properties of GAPR-1 in combination with existing knowledge on CAP protein structure-function relationships. We propose that the CAP domain is a structural domain, which can regulate protein-protein interactions of CAP family members using its amyloidogenic properties.
- CAP superfamily,
- GAPR-1,
- oligomer,
- amyloid,
- reproduction,
- immune regulation
Citation: Nick K. Olrichs, J. Bernd Helms. Novel insights into the function of the conserved domain of the CAP superfamily of proteins[J]. AIMS Biophysics, 2016, 3(2): 232-246. doi: 10.3934/biophy.2016.2.232

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Abstract

Members of the Cysteine-rich secretory proteins, Antigen 5, and Pathogenesis-related 1 proteins (CAP) superfamily are found in a remarkable variety of biological species. The presence of a highly conserved CAP domain defines the CAP family members, which in many cases is linked to other functional protein domains. As a result, this superfamily of proteins is involved in a large variety of biological processes such as reproduction, tumor suppression, and immune regulation. The role of the CAP domain and its conserved structure throughout evolution in relation to the diverse functions of CAP proteins is, however, poorly understood. Recent studies on the mammalian Golgi-Associated plant Pathogenesis Related protein 1 (GAPR-1), which consists almost exclusively of a CAP domain, may shed new light on the function of the CAP domain. GAPR-1 was shown to form amyloid fibrils but also to possess anti-amyloidogenic properties against other amyloid forming peptides. Amyloid prediction analysis reveals the presence of potentially amyloidogenic sequences within the highly conserved sequence motifs of the CAP domain. This review will address the structural properties of GAPR-1 in combination with existing knowledge on CAP protein structure-function relationships. We propose that the CAP domain is a structural domain, which can regulate protein-protein interactions of CAP family members using its amyloidogenic properties.

References

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