CAMSAP2

CAMSAP2
Identifiers
AliasesCAMSAP2, CAMSAP1L1, calmodulin regulated spectrin associated protein family member 2
External IDsOMIM: 613775; MGI: 1922434; HomoloGene: 18927; GeneCards: CAMSAP2; OMA:CAMSAP2 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001297707
NM_001297708
NM_203459
NM_001389638

NM_001081360
NM_001347109
NM_001347110

RefSeq (protein)

NP_001284636
NP_001284637
NP_982284

NP_001334038
NP_001334039

Location (UCSC)Chr 1: 200.74 – 200.86 MbChr 1: 136.2 – 136.27 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Calmodulin-regulated spectrin-associated protein family member 2 (CAMSAP2) is a protein in humans that is encoded by the CAMSAP2 gene.[5] CAMSAP2 possesses a microtubule-binding domain near the C-terminal region where "microtubule interactions" occur. On the C-terminal regions, protein to protein interactions are accelerated by three coiled-coil domains, which function as molecular spacers.[6] CAMSAP2 acts as a microtubule minus-end anchor and binds microtubules through its CKK domain. CAMSAP2 is necessary for the proper organization and stabilization of interphase microtubules. The protein also plays a role in cell migration.[7] CAMSAP2 stabilizes and attaches microtubule minus ends to the Golgi through the AKAP9 complex and myomegalin. CLASP1 proteins are responsible for microtubule stability which are not required for the Golgi tethering. When no centromeres are present, AKAP9 and CAMSAP-2 dependent pathways of the microtubule minus ends become a dominant force and must exist in order to observe the maintenance of microtubule density.[8]

3D rendering of the CAMSAP2 protein.[9][10][11]
  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000118200Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000041570Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ "CAMSAP2 calmodulin regulated spectrin associated protein family member 2 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Archived from the original on 2024-02-27. Retrieved 2024-03-11.
  6. ^ Mao BP, Ge R, Cheng CY (January 2020). "Role of microtubule +TIPs and -TIPs in spermatogenesis - Insights from studies of toxicant models". Reproductive Toxicology. 91: 43–52. doi:10.1016/j.reprotox.2019.11.006. PMID 31756440. Archived from the original on 2024-04-15. Retrieved 2024-04-15.
  7. ^ Baines AJ, Bignone PA, King MD, Maggs AM, Bennett PM, Pinder JC, et al. (September 2009). "The CKK domain (DUF1781) binds microtubules and defines the CAMSAP/ssp4 family of animal proteins". Molecular Biology and Evolution. 26 (9): 2005–2014. doi:10.1093/molbev/msp115. PMID 19508979. Archived from the original on 2022-06-15. Retrieved 2022-09-29.
  8. ^ Wu J, de Heus C, Liu Q, Bouchet BP, Noordstra I, Jiang K, et al. (October 2016). "Molecular Pathway of Microtubule Organization at the Golgi Apparatus". Developmental Cell. 39 (1): 44–60. doi:10.1016/j.devcel.2016.08.009. PMID 27666745. Archived from the original on 2024-04-15. Retrieved 2024-04-15.
  9. ^ "AlphaFold Protein Structure Database". alphafold.ebi.ac.uk. Archived from the original on 2022-10-01. Retrieved 2024-04-12.
  10. ^ Varadi M, Anyango S, Deshpande M, Nair S, Natassia C, Yordanova G, et al. (January 2022). "AlphaFold Protein Structure Database: massively expanding the structural coverage of protein-sequence space with high-accuracy models". Nucleic Acids Research. 50 (D1): D439–D444. doi:10.1093/nar/gkab1061. PMC 8728224. PMID 34791371. Archived from the original on 2024-04-15. Retrieved 2024-04-15.
  11. ^ Jumper J, Evans R, Pritzel A, Green T, Figurnov M, Ronneberger O, et al. (August 2021). "Highly accurate protein structure prediction with AlphaFold". Nature. 596 (7873): 583–589. Bibcode:2021Natur.596..583J. doi:10.1038/s41586-021-03819-2. PMC 8371605. PMID 34265844.