The Amino-Terminal Hydrophobic Region of the Small Subunit of Calcium-Activated Neutral Protease (CANP) Is Essential for Its Activation by Phosphatidylinositol1

Imajoh, Shinobu; Kawasaki, Hiroshi; Suzuki, Koichi

doi:10.1093/oxfordjournals.jbchem.a135593

Cited by 113 publications

(54 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…No significant effects on headgroup selectivity were observed. Previous reports (Imajoh et al, 1986;Crawford et al, 1990;Arthur and Crawford, 1996) suggesting a role for domain V in the interaction of the calpains with membranes were confirmed and extended by our quantitative data. Interestingly, even for the (D405A)Lq(DV)S variant, in which the contribution of domain V is eliminated, the additional acidic loop D405A mutation had no significant effect on lipid binding affinity (Table 3).…”

Section: Deletion Of Domain V Lowers the Membrane Affinity Of The Hetsupporting

confidence: 89%

“…Domain V is an unusual, hydrophobic, Gly-rich sequence that did not diffract in X-ray crystallography (Strobl et al, 2000). Studies with calpains lacking domain V, as well as with synthetic peptides mimicking parts of this domain, suggested a role of domain V in the interaction of calpain with membranes (Imajoh et al, 1986;Crawford et al, 1990;Arthur and Crawford, 1996;Brandenburg et al, 2002;Dennison et al, 2005). Domain III weakly resembles C2 domains, which are Ca 2q -and phospholipid-binding modules found in a number of signalling and membrane trafficking proteins (Rizo and Sudhof, 1998;Cho, 2001).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

μ-Calpain binds to lipid bilayers via the exposed hydrophobic surface of its Ca2+-activated conformation

Fernández-Montalván

Assfalg-Machleidt²,

Pfeiler³

et al. 2006

Biological Chemistry

View full text Add to dashboard Cite

active-site mutated heterodimeric human m-calpain with phospholipid bilayers was studied in vitro using proteinto-lipid fluorescence resonance energy transfer and surface plasmon resonance. Binding to liposomes was Ca 2q -dependent, but not selective for specific phospholipid head groups. wCa 2q x 0.5 for association with lipid bilayers was not lower than that required for the exposure of hydrophobic surface (detected by TNS fluorescence) or for enzyme activity in the absence of lipids. Deletion of domain V reduced the lipid affinity of the isolated small subunit (600-fold) and of the heterodimer (10-to 15-fold), thus confirming the proposed role of domain V for membrane binding. Unexpectedly, mutations in the acidic loop of the 'C2-like' domain III, a putative Ca 2q and phospholipid-binding site, did not affect lipid affinity. Taken together, these results support the hypothesis that in vitro membrane binding of m-calpain is due to the exposed hydrophobic surface of the active conformation and does not reduce the Ca 2q requirement for activation.

show abstract

Section: Deletion Of Domain V Lowers the Membrane Affinity Of The Hetsupporting

confidence: 89%

Section: Introductionmentioning

confidence: 99%

μ-Calpain binds to lipid bilayers via the exposed hydrophobic surface of its Ca2+-activated conformation

Fernández-Montalván

Assfalg-Machleidt²,

Pfeiler³

et al. 2006

Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…ApoA-I failed to increase ABCA1-W590S levels in these studies, suggesting that apoA-I binding was not sufficient for ABCA1 stabilization (36). These results favor the hypothesis that apoA-I-mediated ABCA1 stabilization may result from local changes in membrane phospholipids that decrease the binding of ABCA1 with the calpain subunit (39). Another interpretation is that apoA-I fails to bind the W590S mutant in the correct orientation, and therefore the appropriate conformational change of ABCA1 required to decrease calpain proteolysis does not occur.…”

Section: The Reciprocal Response Of the Binding Of Apoa-i/abca1mentioning

confidence: 51%

The Interaction of ApoA-I and ABCA1 Triggers Signal Transduction Pathways to Mediate Efflux of Cellular Lipids

Zhao

Yin

et al. 2011

Mol Med

View full text Add to dashboard Cite

Reverse cholesterol transport (RCT) has been characterized as a crucial step for antiatherosclerosis, which is initiated by ATPbinding cassette A1 (ABCA1) to mediate the efflux of cellular phospholipids and cholesterol to lipid-free apolipoprotein A-I (apoA-I). However, the mechanisms underlying apoA-I/ABCA1 interaction to lead to the lipidation of apoA-I are poorly understood. There are several models proposed for the interaction of apoA-I with ABCA1 as well as the lipidation of apoA-I mediated by ABCA1. ApoA-I increases the levels of ABCA1 protein markedly. In turn, ABCA1 can stabilize apoA-I. The interaction of apoA-I with ABCA1 could activate signaling molecules that modulate posttranslational ABCA1 activity or lipid transport activity. The key signaling molecules in these processes include protein kinase A (PKA), protein kinase C (PKC), Janus kinase 2 (JAK2), Rho GTPases and Ca 2+ , and many factors also could influence the interaction of apoA-I with ABCA1. This review will summarize these mechanisms for the apoA-I interaction with ABCA1 as well as the signal transduction pathways involved in these processes.

show abstract

“…These sequences have been thought to serve in some protein molecules as separators or spacers, or as hinges, between functionally different parts of the molecule (23,24). In cytokeratins, in which they occur at the ends of rodlike molecules, they have been thought to be contact points for interaction with matrix protein (25); and in calcium-activated neutral protease a glycine rich sequence is associated with an interaction of the enzyme with cellular membranes (26). Thus there are multiple potential targets for an EBNA-1 induced autoimmunity, and it seems a certainty that other candidates will appear over time, The anti-p542 autoantibodv respon.se.…”

Section: Discussionmentioning

confidence: 99%

Epstein-Barr virus-induced autoimmune responses. I. Immunoglobulin M autoantibodies to proteins mimicking and not mimicking Epstein-Barr virus nuclear antigen-1.

Vaughan

Valbracht²,

Nguyen³

et al. 1995

J. Clin. Invest.

View full text Add to dashboard Cite

In previous studies of infectious mononucleosis, we found IgM autoantibodies which react with hematopoietic cell antigens. Many of these were inhibited by synthetic glycine/ alanine peptides representing the glycine/alanine repeat of Epstein-Barr virus nuclear antigen-i. We have cloned and expressed fragments of genes encoding two of these autoantigens. One gene (p542) encodes a protein containing a glycine-rich 28-mer, which is its chief autoantigenic epitope and which represents a newly identified class of evolutionarily conserved autoepitopes. The other gene (p554) encodes a protein that is not demonstrably cross-reactive with EpsteinBarr virus nuclear antigen-1 or with any other EBV protein, but forms complexes with other proteins. Immunoaffinitypurified anti-p542 and anti-p554 have relatively high binding affinities, as evidenced by inhibition at 106-108 M-', and neither autoantibody showed polyreactivity with other common antigens. The data thus suggest that neither autoantibody is simply an expression of polyclonal B cell activation. We conclude that the two autoantigens stimulate autoantibody synthesis by different mechanisms. One autoantigen shares homology to a viral protein which generates cross-reacting antibodies to the autoantigenic epitope. The other has no recognizable cross-reaction with the infecting pathogen and may become immunogenic through complexing with other proteins. (J. Clin. Invest. 1995Invest. . 95:1306Invest. -1315

show abstract

The Amino-Terminal Hydrophobic Region of the Small Subunit of Calcium-Activated Neutral Protease (CANP) Is Essential for Its Activation by Phosphatidylinositol1

Cited by 113 publications

References 0 publications

μ-Calpain binds to lipid bilayers via the exposed hydrophobic surface of its Ca2+-activated conformation

μ-Calpain binds to lipid bilayers via the exposed hydrophobic surface of its Ca2+-activated conformation

The Interaction of ApoA-I and ABCA1 Triggers Signal Transduction Pathways to Mediate Efflux of Cellular Lipids

Epstein-Barr virus-induced autoimmune responses. I. Immunoglobulin M autoantibodies to proteins mimicking and not mimicking Epstein-Barr virus nuclear antigen-1.

Contact Info

Product

Resources

About