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. 1998 Feb 9;140(3):603–616. doi: 10.1083/jcb.140.3.603

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(A and B) HRP distribution in cells expressing ARF6(Q67L) and ARF6(T27N). Cells expressing ARF6(Q67L) (A) and ARF6(T27N) (B) were incubated with HRP for 60 min, fixed, and then processed for ultrathin cryosections. Sections were first labeled with anti-ARF6 antibody followed by protein A–conjugated gold particles (10 nm) and then with an anti-HRP antibody followed by protein A–gold particles (5 nm). (A) Typically, in ARF6 (Q67L)-expressing cells, HRP labeling was restricted to small vesicles at the periphery (e). Membrane invaginations were observed even at very low levels of ARF6(Q67L) expression, implicit by low numbers of gold particles on the membrane. (B) A small population of ARF6(T27N)-positive vesicles were also labeled with HRP (arrows). i, invaginations; e, endosomes; p, plasma membrane. Bar, 200 nm.

(A and B) HRP distribution in cells expressing ARF6(Q67L) and ARF6(T27N). Cells expressing ARF6(Q67L) (A) and ARF6(T27N) (B) were incubated with HRP for 60 min, fixed, and then processed for ultrathin cryosections. Sections were first labeled with anti-ARF6 antibody followed by protein A–conjugated gold particles (10 nm) and then with an anti-HRP antibody followed by protein A–gold particles (5 nm). (A) Typically, in ARF6 (Q67L)-expressing cells, HRP labeling was restricted to small vesicles at the periphery (e). Membrane invaginations were observed even at very low levels of ARF6(Q67L) expression, implicit by low numbers of gold particles on the membrane. (B) A small population of ARF6(T27N)-positive vesicles were also labeled with HRP (arrows). i, invaginations; e, endosomes; p, plasma membrane. Bar, 200 nm.