Phosphoinositides in membranes that build up the triads of rabbit skeletal muscle

Milting, Hendrik; Heilmeyer, Ludwig; Thieleczek, Rolf

doi:10.1016/0014-5793(94)00440-4

Cited by 17 publications

(19 citation statements)

References 36 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…When we degraded PI(4,5)P 2 , dysferlin could no longer induce tubule formations in non-muscle cells, indicating that the presence of PI(4,5)P 2 is an essential requirement for dysferlindependent T-tubule formation. This finding is in agreement with the enrichment of PI(4,5)P 2 in T-tubules (Lee et al, 2002;Milting et al, 1994). We could show that PI(4,5)P 2 depletion also altered the T-tubule system in C2C12 myotubes, reinforcing the link between dysferlin-dependent phospholipid binding and the biogenesis of the T-tubule system.…”

Section: Dysferlin Tubulates Membranes In Vitro and In Cellular Systemssupporting

confidence: 90%

“…Lipid specificity of dysferlin T-tubules of striated muscle are enriched in PI(4,5)P 2 , and this phospholipid also marks the sites of Bin1 activity (Lee et al, 2002;Milting et al, 1994;Wu and Baumgart, 2014). In addition, the individual C2 domains of dysferlin are known to bind to phospholipids (Davis et al, 2002;Therrien et al, 2009).…”

Section: Dysferlin Mediates Membrane Tubulation In Vivo and In Vitromentioning

confidence: 99%

See 1 more Smart Citation

Dysferlin mediates membrane tubulation and links T-tubule biogenesis to muscular dystrophy

Hofhuis¹,

Bersch²,

Büssenschütt³

et al. 2017

Journal of Cell Science

View full text Add to dashboard Cite

The multi-C2 domain protein dysferlin localizes to the plasma membrane and the T-tubule system in skeletal muscle; however, its physiological mode of action is unknown. Mutations in the DYSF gene lead to autosomal recessive limb-girdle muscular dystrophy type 2B and Miyoshi myopathy. Here, we show that dysferlin has membrane tubulating capacity and that it shapes the T-tubule system. Dysferlin tubulates liposomes, generates a T-tubule-like membrane system in non-muscle cells, and links the recruitment of phosphatidylinositol 4,5-bisphosphate to the biogenesis of the T-tubule system. Pathogenic mutant forms interfere with all of these functions, indicating that muscular wasting and dystrophy are caused by the dysferlin mutants' inability to form a functional T-tubule membrane system.

show abstract

Section: Dysferlin Tubulates Membranes In Vitro and In Cellular Systemssupporting

confidence: 90%

Section: Dysferlin Mediates Membrane Tubulation In Vivo and In Vitromentioning

confidence: 99%

Dysferlin mediates membrane tubulation and links T-tubule biogenesis to muscular dystrophy

Hofhuis¹,

Bersch²,

Büssenschütt³

et al. 2017

Journal of Cell Science

View full text Add to dashboard Cite

show abstract

“…the presence of phosphatidylinositol, phosphatidylserine or phosphatidic acid at low mole fractions has no effect on activity, and at higher mole fractions leads to inhibition [23]. The native SR membrane contains about 2 mol % phosphatidylserine and 8 mol % of PtdIns and PtdIns(4)P, but no PtdIns(4,5)P # [29,30]. The absence of PtdIns(4,5)P # means that SR lacks the capacity for Ins(1,4,5)P $ generation [30].…”

Section: Figure 6 Simulations Of Ca 2 + Accumulationmentioning

confidence: 99%

“…The native SR membrane contains about 2 mol % phosphatidylserine and 8 mol % of PtdIns and PtdIns(4)P, but no PtdIns(4,5)P # [29,30]. The absence of PtdIns(4,5)P # means that SR lacks the capacity for Ins(1,4,5)P $ generation [30].…”

Section: Figure 6 Simulations Of Ca 2 + Accumulationmentioning

confidence: 99%

“…The observation that the optimal concentration of anionic phospholipid (10 mol %) equals the mole fraction of anionic phospholipid in the native SR membrane [29,30] suggests that reducing slippage might be important for the physiological function of the Ca# + -ATPase. The observation that PtdIns(4)P is more effective in reducing slippage than is PtdIns suggests a possible mechanism for control of the Ca# + accumulation by the ATPase ; PtdIns-4-kinase has been detected in SR, as has a Ca# + -dependent phosphomonoesterase capable of catalysing the breakdown of PtdIns(4)P [43,44].…”

mentioning

confidence: 99%

See 1 more Smart Citation

Anionic phospholipids decrease the rate of slippage on the Ca2+-ATPase of sarcoplasmic reticulum

Dalton

Pilot

Mall

et al. 1999

Biochemical Journal

View full text Add to dashboard Cite

Accumulation of Ca2+ by the Ca2+-ATPase of skeletal-muscle sarcoplasmic reticulum has been measured in reconstituted, sealed vesicles as a function of lipid composition. Measurements were performed in the presence of carbonyl cyanide p-trifluoromethoxyphenylhydrazone (FCCP) to eliminate any effects of H+ transport; in the presence of FCCP, addition of valinomycin had no effect on the level or rate of accumulation of Ca2+ showing that, in the presence of FCCP, no electrical potential built up across the membrane. Levels of accumulation were low when the phospholipid was dioleoylphosphatidylcholine (DOPC), even though DOPC supports high ATPase activity. Inclusion of 10 mol% anionic phospholipid [dioleoylphosphatidic acid (DOPA) or dioleoylphosphatidylserine (DOPS)] led to higher levels of accumulation of Ca2+, 10 mol% being the optimum concentration. Cardiolipin or phosphatidylinositol 4-phosphate were more effective than DOPA or DOPS in increasing accumulation of Ca2+. Effects of anionic phospholipids were seen in the presence of an ATP-regenerating system to remove ADP, and in the presence of phosphate within the reconstituted vesicles to precipitate calcium phosphate. Rates of passive leak of Ca2+ from the reconstituted vesicles were slow. The Ca2+-accumulation process was simulated assuming either simple passive leak of Ca2+ from the vesicles or assuming slippage on the ATPase, a process in which the phosphorylated intermediate of the ATPase releases bound Ca2+ on the cytoplasmic rather than the lumenal side of the membrane. The experimental data fitted to a slippage model, with anionic phospholipids decreasing the rate of slippage.

show abstract

Isolation of T‐Tubules from Skeletal Muscle

Zorzano

Camps

2006

CP Cell Biology

View full text Add to dashboard Cite

The transverse tubules (T‐tubules) of mammalian cardiac and skeletal muscles are invaginations of the sarcolemma. They play a crucial role in excitation‐contraction coupling as well as in intracellular signaling and in regulation of glucose transport. The biochemical purification of T‐tubule membranes is a difficult task, and membrane fractions enriched in transverse tubules are usually contaminated with other cell‐surface and intracellular membranes. This unit includes methods that permit the isolation and purification of T‐tubules from skeletal muscle.

show abstract

Phosphoinositides in membranes that build up the triads of rabbit skeletal muscle

Cited by 17 publications

References 36 publications

Dysferlin mediates membrane tubulation and links T-tubule biogenesis to muscular dystrophy

Dysferlin mediates membrane tubulation and links T-tubule biogenesis to muscular dystrophy

Anionic phospholipids decrease the rate of slippage on the Ca2+-ATPase of sarcoplasmic reticulum

Isolation of T‐Tubules from Skeletal Muscle

Contact Info

Product

Resources

About