Jump to content

CAPZA2: Difference between revisions

From Wikipedia, the free encyclopedia
Browse history interactively
← Previous editNext edit →
Content deleted Content added
VisualWikitext
function
interactions
Line 7: Line 7:
== Function ==
== Function ==
CapZ binds the barbed end of [[actin]] filaments and prevents addition or loss of [[actin]] monomers to filaments. It has also been observed that CapZ functions to organize [[myofilament]]s during myofibrillogenesis and is present at [[Z-disc]]s in muscle prior to the striation of [[actin]] filaments, suggesting that CapZ may function to direct the polarity and organization of [[sarcomere|sarcomeric]] [[actin]] during [[sarcomere#bands|I-band]] formation.<ref>{{cite journal|last1=Schafer|first1=DA|last2=Waddle|first2=JA|last3=Cooper|first3=JA|title=Localization of CapZ during myofibrillogenesis in cultured chicken muscle.|journal=Cell motility and the cytoskeleton|date=1993|volume=25|issue=4|pages=317-35|pmid=8402953}}</ref>
CapZ binds the barbed end of [[actin]] filaments and prevents addition or loss of [[actin]] monomers to filaments. It has also been observed that CapZ functions to organize [[myofilament]]s during myofibrillogenesis and is present at [[Z-disc]]s in muscle prior to the striation of [[actin]] filaments, suggesting that CapZ may function to direct the polarity and organization of [[sarcomere|sarcomeric]] [[actin]] during [[sarcomere#bands|I-band]] formation.<ref>{{cite journal|last1=Schafer|first1=DA|last2=Waddle|first2=JA|last3=Cooper|first3=JA|title=Localization of CapZ during myofibrillogenesis in cultured chicken muscle.|journal=Cell motility and the cytoskeleton|date=1993|volume=25|issue=4|pages=317-35|pmid=8402953}}</ref>

== Clinical Significance ==


== Interactions ==
CapZ-alpha2 has been shown to [[protein-protein interaction|interact]] with:

* [[ACTA1]]<ref>{{cite journal|last1=Schafer|first1=DA|last2=Waddle|first2=JA|last3=Cooper|first3=JA|title=Localization of CapZ during myofibrillogenesis in cultured chicken muscle.|journal=Cell motility and the cytoskeleton|date=1993|volume=25|issue=4|pages=317-35|pmid=8402953}}</ref>
* [[ACTC1]]<ref>{{cite journal|last1=Schafer|first1=DA|last2=Waddle|first2=JA|last3=Cooper|first3=JA|title=Localization of CapZ during myofibrillogenesis in cultured chicken muscle.|journal=Cell motility and the cytoskeleton|date=1993|volume=25|issue=4|pages=317-35|pmid=8402953}}</ref>
* [[S100A1]]<ref>{{cite journal|last1=Ivanenkov|first1=VV|last2=Dimlich|first2=RV|last3=Jamieson GA|first3=Jr|title=Interaction of S100a0 protein with the actin capping protein, CapZ: characterization of a putative S100a0 binding site in CapZ alpha-subunit.|journal=Biochemical and biophysical research communications|date=5 April 1996|volume=221|issue=1|pages=46-50|pmid=8660341}}</ref>




Revision as of 15:31, 21 September 2015

Template:PBB F-actin-capping protein subunit alpha-2 also known as CapZ-alpha2 is a protein that in humans is encoded by the CAPZA2 gene.[1]

Structure

CapZ-alpha2 is a 33.0 kDa protein comprised of 286 amino acids.[2] CAPZA2 is located on human chromosome 7, position q31.2-q31.3.[3] The primary sequence of CapZ-alpha2 contains three C-terminal, regularly spaced leucines at positions 258, 262 and 266 found in consensus sequence of KxxxLxxE/DLxxALxxK/R that are critical for actin binding; these residues are conserved within the CapZ-beta isoform..[3] CapZ-alpha2 is 85% identical to CapZ-alpha1, and differ by a small number of key amino acids; 21 amino acid differences perpetrate isoform specificity.[4] CapZ-alpha2 is expressed in a variety of tissues, including cardiac muscle and skeletal muscle, where it caps sarcomeric actin at Z-discs; the ratio of CapZ-alpha2 to CapZ-alpha1 varies significantly among different tissues.[4]

Function

CapZ binds the barbed end of actin filaments and prevents addition or loss of actin monomers to filaments. It has also been observed that CapZ functions to organize myofilaments during myofibrillogenesis and is present at Z-discs in muscle prior to the striation of actin filaments, suggesting that CapZ may function to direct the polarity and organization of sarcomeric actin during I-band formation.[5]

Clinical Significance

Interactions

CapZ-alpha2 has been shown to interact with:


References

  1. ^ "Entrez Gene: CAPZA2 capping protein (actin filament) muscle Z-line, alpha 2".
  2. ^ "Protein sequence of human CAPZA2 (Uniprot ID: P47755)". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB). Retrieved 18 September 2015.
  3. ^ a b Barron-Casella EA, Torres MA, Scherer SW, Heng HH, Tsui LC, Casella JF (Sep 1995). "Sequence analysis and chromosomal localization of human Cap Z. Conserved residues within the actin-binding domain may link Cap Z to gelsolin/severin and profilin protein families". The Journal of Biological Chemistry. 270 (37): 21472–9. PMID 7665558.
  4. ^ a b Hart MC, Korshunova YO, Cooper JA (1997). "Vertebrates have conserved capping protein alpha isoforms with specific expression patterns". Cell Motility and the Cytoskeleton. 38 (2): 120–32. doi:10.1002/(SICI)1097-0169(1997)38:2<120::AID-CM2>3.0.CO;2-B. PMID 9331217.
  5. ^ Schafer, DA; Waddle, JA; Cooper, JA (1993). "Localization of CapZ during myofibrillogenesis in cultured chicken muscle". Cell motility and the cytoskeleton. 25 (4): 317–35. PMID 8402953.
  6. ^ Schafer, DA; Waddle, JA; Cooper, JA (1993). "Localization of CapZ during myofibrillogenesis in cultured chicken muscle". Cell motility and the cytoskeleton. 25 (4): 317–35. PMID 8402953.
  7. ^ Schafer, DA; Waddle, JA; Cooper, JA (1993). "Localization of CapZ during myofibrillogenesis in cultured chicken muscle". Cell motility and the cytoskeleton. 25 (4): 317–35. PMID 8402953.
  8. ^ Ivanenkov, VV; Dimlich, RV; Jamieson GA, Jr (5 April 1996). "Interaction of S100a0 protein with the actin capping protein, CapZ: characterization of a putative S100a0 binding site in CapZ alpha-subunit". Biochemical and biophysical research communications. 221 (1): 46–50. PMID 8660341.

Further reading

  • Dawson SJ, White LA (May 1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". The Journal of Infection. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. PMID 1602151.
  • Maruyama K, Sugano S (Jan 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Hart MC, Korshunova YO, Cooper JA (1997). "Vertebrates have conserved capping protein alpha isoforms with specific expression patterns". Cell Motility and the Cytoskeleton. 38 (2): 120–32. doi:10.1002/(SICI)1097-0169(1997)38:2<120::AID-CM2>3.0.CO;2-B. PMID 9331217.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Miyagawa Y, Tanaka H, Iguchi N, Kitamura K, Nakamura Y, Takahashi T, Matsumiya K, Okuyama A, Nishimune Y (Jun 2002). "Molecular cloning and characterization of the human orthologue of male germ cell-specific actin capping protein alpha3 (cpalpha3)". Molecular Human Reproduction. 8 (6): 531–9. doi:10.1093/molehr/8.6.531. PMID 12029070.
  • Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J (May 2003). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nature Biotechnology. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.
  • Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
Retrieved from "https://en.wikipedia.org/w/index.php?title=CAPZA2&oldid=682103616"