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Na + /P i co-transport alters rapidly cytoskeletal protein polymerization dynamics in opossum kidney cells

We studied with biochemical and immunoﬂuorescent techniques the interactions between the actin microﬁlament and tubulin microtubule cytoskeleton and Na + (cid:125) P i co-transport in opossum kidney cells, a line with proximal tubular characteristics. On brief (5 min) incubation of the cells with a low (0.1 mM) concentration of P i , a rapid F-actin depolymerization takes place, which fails to occur in cells incubated under similar conditions with 1 mM P i . The disassembly of actin microﬁlaments could be quantitatively expressed as a 33 % increase in the ratio of monomeric G-actin to polymerized F-actin (G (cid:125) F-actin ratio from 0.80 (cid:179) 0.03 to 1.06 (cid:179) 0.06, n (cid:175) 28, P (cid:33) 0.01), owing to a signiﬁcant decrease in the latter. Under these conditions microﬁlaments were also markedly destabilized, as shown by their diminished resistance to graded cytochalasin B concentrations. In addition, incubation of opossum kidney cells with low P i concentrations (0.1 mM) resulted within 5 min in a substantial depolymerization of microtubules, shown by immunoﬂuorescence microscopy and measured as a 70.9 (cid:179) 6.9 % ( n (cid:175) 11, P (cid:33) 0.01)