Nuclear membrane proteins

Ansari, B., Dover, R., Gillmore, C. P., and Hall, P. A. 1993. Expression of the nuclear membrane protein statin in cycling cells. J. Pathol. 769 391-396. 

ORGANELLE PROTEOME VARIATION AMONG DIFFERENT CELL TYPES LESSONS FROM NUCLEAR MEMBRANE PROTEINS... 

Bengtsson, L. and Wilson, K.L. (2004) Multiple and surprising new functions for emerin, a nuclear membrane protein. Curr. Opin. Cell Biol. 16,73-79. 

Brachner, A., Reipert, S., Foisner, R. and Gotzmann, J. (2005) LEM2 is a novel MANl-related inner nuclear membrane protein associated with A-type lamins. J. Cell Sci. 118, 5797-5810. 

Ellenberg, J., Siggia, E.D., Moreira, J.E., Smith, C.L., Presley, J.F., Worman, H.J. and Lippincott-Schwartz, J. (1997) Nuclear membrane dynamics and reassembly in living cells targeting of an inner nuclear membrane protein in interphase and mitosis. J. Cell. Biol. 138, 1193-1206. 

Lin, F, Blake, D.L., Callebaut, I., Skeijanc, I.S., Holmer, L., McBumey, M.W., Paulin-Levasseur, M. and Worman, H.J. (2000) MANl, an inner nuclear membrane protein that shares the LEM domain with lamina-associated polypeptide 2 andemerin. J. Biol. Chem. 275, 4840-4847. 

Manilal, S., Nguyen, T.M., Sewry, C.A. and Morris, G.E. (1996) The Emery-Dreifuss muscular dystrophy protein, emerin, is a nuclear membrane protein. Hum. Mol. Genet. 5, 801-808. 

Schirmer, E.C., Florens, L., Guan, T, Yates, J.R. 3rd and Gerace, L. (2003) Nuclear membrane proteins with potential disease links found by subtractive proteomics. Science 301, 1380-1382. 

Wilhelmsen, K., Litjens, S.H., Kuikman, L, Tshimbalanga, N., Janssen, H., van den Bout, I., Raymond, K. and Sonnenberg, A. (2005) Nesprin-3, a novel outer nuclear membrane protein, associates with the cytoskeletal linker protein plectin. J. Cell Biol. 171, 799-810. 

The fall in MPF activity in telophase allows constitutive protein phosphatases to remove the regulatory phosphates from condensln, lamlns, nucleoporlns, and other nuclear membrane proteins, permitting the decondensation of chromosomes and the reassembly of the nuclear membrane, nuclear lamina, and nuclear pore complexes. 

FIGURE 20.3 Schematic representation of the differential detergent fractionation procedure applied to cultured cells. Four fractions are obtained (1) cytosolic proteins, (2) membrane/organelle proteins, (3) nuclear-membrane proteins, and (4) cytoskeletal proteins. (Modified from Fazal, M. A., et al., J. Chwmatogr. A, 1130, 182-189,2006.)... 

FIG U RE 20.5 Two-dimensional eleciropherogtams of each differential detergent fraction. The digitonin fraction (A) is the cytosolic proteins, the Triton fraction (B) is the membrane/organelle proteins, the Tween fraction (C) is the nuclear-membrane proteins, and the detergent resistant fraction (D) is the eytoskeletal proteins. (Reprinted from Fazal,M. A., etal.,7. Chromatogr. A, 1130,182-189, 2006. Copyright 2006. With permission from Elsevier.)... 

Simos, G., and Georgatos, S. D. (1992). The inner nuclear membrane protein p58 associates in vivo with a p58 kinase and the nuclear lamins. EMBO J. 11, 4027-4036. 

This procedure is not stringent and leaves integral and peripheral nuclear membrane proteins in the preparation. Preparations enriched in integral membrane proteins can be obtained following a salt wash (J.-C. Courvalin, personal communication, adapted from Dwyer and Blobel, 1976). The nuclear envelope pellet is resuspended in 300 /xl of 0.5 M NaCl, 20 mM Tris-HCl (pH 7.5) and left on ice for 10 min. The suspension is centrifuged at 10,000 g for 10 min through a 100-/xl sucrose/NaCl cushion (20% sucrose, 20 mM Tris-HCl, pH 7.5, 0.25 M NaCl). The pellet is resuspended in TN. 

FLAP and LTC synthase are shown as int ral nuclear membrane proteins, with a phospholipase (PL) associating with this membrane to release AA Following the release ofAA, 5-LOX (S LO) translocates to the nuclear membrane in a process r dated by FLAP. S-LQX then converts M into LTA which is subsequently converted into LTC by LTC synthase. LTC is exported from the cell by a membrane carrier [60]. Points at which this process can be inhibited are indicated (1-5 blockade of PL, FLAP, 5-LOX, LTC synthase and the carrier protein respectively). 

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